Acrobatic duo in the cells
The protein Trigger factor recognizes a partner with unstable domains to form a stable protein duo. Chaperones like TF help folding of other proteins.
Protein Domains
Articles tagged with Protein Domains
What a rare blood disease can teach us about blood clotting
Researchers discovered a previously unknown region of antithrombin protein plays a crucial role in preventing blood clots. This finding could lead to better-designed drugs for other blood disorders and improved treatments for patients with antithrombin deficiency.
SourceAmerican Society for Biochemistry and Molecular Biology·JournalJournal of Biological Chemistry·DateOct 2, 2017
UMass Amherst biochemists simulate a protein-folding chaperone's functional dance
Researchers at UMass Amherst have characterized the functional dance of a protein-folding chaperone's interdomain linker. The study used computational techniques to simulate the movement of the linker and revealed its role in facilitating proper function, including binding sites for potential therapeutic targets.
Photo-responsive protein hydrogels as agent for controlled stem cell/protein release
Researchers from HKUST created a B12-dependent light-sensing hydrogel by covalently stitching together photoreceptor proteins, enabling rapid gel-sol transition on light exposure. This allows for controlled release of stem cells and proteins with high spatiotemporal precision.
SourceHong Kong University of Science and Technology·JournalProceedings of the National Academy of Sciences·DateJul 6, 2017
Kinky biology
Using supercomputer simulations, researchers have discovered that kinks in DNA can significantly reduce energy and pressure, allowing it to fit into a micron-sized space. The findings provide new insights into how cells pack DNA and could lead to advances in understanding biological phenomena.
SourceUniversity of Texas at Austin, Texas Advanced Computing Center·JournalJournal of Computational Chemistry·DateJul 6, 2017
New statistical analysis reveals thousands of rare mutations linked with cancer
Scientists have discovered thousands of rare genetic mutations contributing to cancer growth, focusing on shared protein domains. These findings could guide the development of treatments targeting multiple mutated proteins simultaneously.
Study reveals the multitasking secrets of an RNA-binding protein
Researchers uncover how a fruit fly protein binds to multiple types of RNA, revealing new insights into its multifunctional role. The study may help explain the diverse functions of RNA-binding proteins implicated in cancer and neurodegenerative diseases.
Evolutionary advantage of the common periwinkle
The common periwinkle has evolved a unique strategy for detoxifying heavy metals, featuring a three-domain metallothionein with increased binding capacity. This adaptation enables the snail to thrive in polluted environments.
Surprising culprit in nerve cell damage identified
Scientists at WashU Medicine have implicated SARM1 in the self-destruction of axons, a process that leads to nerve cell damage in neurodegenerative diseases. The study suggests that blocking this pathway could slow or prevent disease progression and has implications for treating peripheral neuropathy.
A new way to reset gene expression in cancer cells shows promise for leukemia treatment
Researchers have identified a new class of reader proteins linked to cancer, including leukemia. Disrupting these proteins may lead to effective combination therapies.
Slowly pulling proteins apart reveals unexpected path to stability
Researchers at Duke University used single-molecule force-spectroscopy to study Protein S, a large protein found in nature. They discovered a previously unknown stable conformation made possible by the interaction between two domains, which may help explain why some proteins are more stable than others.
New structure identified in membrane of disease-causing bacteria
Molecular microbiologists at UMass Amherst identify a distinct domain on the plasma membrane of Mycobacterium smegmatis, crucial for bacterial growth. The discovery provides insight into lipid metabolism and regulatory mechanisms in mycobacteria, potentially leading to new methods of inhibiting bacterial growth.
SourceUniversity of Massachusetts Amherst·JournalProceedings of the National Academy of Sciences·DateApr 25, 2016
A cellular sensor of phosphate levels
A region of specific proteins called SPX domain signals the phosphate status to cells, regulating phosphate uptake. InsP signaling molecules interact with SPX domains to control phosphate homeostasis in various organisms.
Breaking the mold: Untangling the jelly-like properties of diseased proteins
Researchers identify reversible phase transitions in FUS protein, leading to aggregation and trapping of other proteins. Disrupting these assemblies can rescue impaired motility and prolong lifespan in ALS models.
Is nature mostly a tinkerer or an inventor?
The University of Miami study reveals that the KLF/SP gene family expanded and diversified during animal evolution through domain shuffling, gene duplication, and de novo domain evolution. This 'tinkering' process led to an increase in repressor domains, which may have contributed to the development of complex cell types and tissues.
Genome-editing proteins seek and find with a slide and a hop
Researchers observed genome-editing proteins using a combination of sliding and hopping to navigate the vast genome. The discovery provides insight into how these proteins can be engineered for improved efficiency and reduced off-target binding, potentially leading to more effective gene therapies.
SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalNature Communications·DateJun 2, 2015
A refined approach to proteins at low resolution
Advances in X-ray technology enabled refinement of previously intractable proteins like the ribosome and viruses. The Deformable Elastic Network (DEN) approach optimizes protein structure prediction by adjusting features to fit diffraction data, reducing ambiguities.
A trigger for muscular diseases
Researchers found that increasing titin's stiffness can be a trigger for pathological changes in skeletal muscles. The team used a mouse model lacking nine titin Ig domains to investigate the effects of increased stiffness, revealing that this can lead to muscle atrophy and contractility changes.
Freeze! A protein group affecting lipid dynamics at cell membranes discovered
Researchers discovered that BAR domain proteins induce strong clustering of phosphoinositides, generating extremely stable protein-lipid scaffolds on the membrane. These scaffolds may contribute to diverse cellular processes by creating lipid phase boundaries and trapping membrane-associated receptor and cargo molecules.
Study offers insight into the origin of the genetic code, team reports
Researchers analyzed aminoacyl tRNA synthetases and found ancient domains linked to dipeptide formation, indicating protein flexibility played a role in genetic code emergence
German and Israeli scientists gain new insights into protein disposal
Researchers found that Cue1 factor contributes to marking defective proteins with molecular tag for degradation, enabling efficient removal. The CUE domain of Cue1 stabilizes ubiquitin chains, regulating formation of degradation signal.
Biologists engineer algae to make complex anti-cancer 'designer' drug
Researchers have genetically engineered algae to produce a complex and expensive human therapeutic drug used to treat cancer. The method could be used to make novel complex designer drugs that can't be produced in any other systems, potentially driving down prices dramatically.
SourceUniversity of California - San Diego·JournalProceedings of the National Academy of Sciences·DateDec 10, 2012
No antibodies, no problem
Mosquitoes use alternative splicing to combine immunoglobulin domains into pathogen-binding proteins, increasing diversity and specificity. This mechanism could lead to new ways to prevent spread of mosquito-borne illnesses like malaria.
Evolutionary increase in size of the human brain explained
The human brain's unique cognitive capacity is attributed to a specific protein domain, DUF1220, which has more copies in humans than other species. The protein's dosage is linked to brain size, with higher numbers associated with macrocephaly and lower numbers with microcephaly.
SourceUniversity of Colorado Anschutz Medical Campus·JournalAmerican Journal of Human Genetics·DateAug 16, 2012
How bacteria change movement direction in response to oxygen: Molecular interactions unravelled
Researchers investigated how bacteria like <i> Bacillus subtilis </i> respond to oxygen changes by studying protein HemAT. The study reveals a signal transduction chain that connects the sensor domain to the signalling domain, allowing the protein to transmit information about rising oxygen levels.
Cell protein interactions favor fats
A study published in Molecular Cell found that more than 30% of PDZ domains interact with various membrane lipids, controlling their cellular location and interaction with other protein partners.
Protein assassin
Scientists have found that the unfolded end of a protein, ColN-T, can still kill E. coli-like bacteria even after its toxic folded portion is removed. This discovery may lead to new, targeted ways to kill antibiotic-resistant microbes.
Let's stretch...
Scientists at EMBL Hamburg have discovered the myomesin protein can stretch up to two-and-a-half times its length, unfolding in a previously unknown way. The study reveals the protein's superhelical architecture and unusual elastic properties, shedding new light on muscle contraction mechanisms.
Cellular processing of proteins found in Congolese child birthing tea now revealed
Researchers have identified the subcellular processing location and target signal of cyclotide kalata B1, a protein found in Congolese child birthing tea. The study reveals that the precursor protein Oak1 is directed to the vacuole through propeptides from the N-terminal region.
Similarities cause protein misfolding
Studies using single-molecule fluorescence reveal that neighboring protein domains with similar amino acid sequences are more prone to misfold, potentially leading to neurodegenerative diseases. This finding suggests that proteins have evolved to limit similarity between domains to prevent misfolding and maintain functionality.
A second pathway for antidepressants
Researchers at Berkeley Lab developed a fluorescent assay that reveals the mechanism of how fluoxetine inhibits TREK1 potassium channels, a key target for antidepressants. The study provides new insights into the molecular mechanisms underlying depression and opens up potential avenues for developing improved treatments.
SourceDOE/Lawrence Berkeley National Laboratory·JournalProceedings of the National Academy of Sciences·DateFeb 7, 2011
New fluorescence technique opens window to protein complexes in living cells
Researchers developed a novel fluorescence anisotropy method to study large protein complexes in real time in live cells. The technique resolves the state of order or disorder of individual protein domains within these complexes, providing new insights into their dynamics and function.
Origins of multicellularity: All in the family
A global collaboration found that Volvox and Chlamydomonas algae share a common list of protein parts, suggesting limited innovation in the transition to multicellularity. Key discoveries include increased ECM proteins, cyclin D proteins, and novel gene functions.
UBC geneticist reveals molecular view of key epigenetic regulator
Researchers at UBC Centre for Molecular Medicine and Therapeutics report detailed structure and function of YEATS domain protein Yaf9, a key player in chromatin regulation. The study reveals conserved function from yeast to humans, shedding light on mechanisms of chromatin modification.
SourceUniversity of British Columbia·JournalProceedings of the National Academy of Sciences·DateDec 9, 2009
Putting the squeeze on sperm DNA
Researchers at EMBL have discovered a new protein, Brdt, that directs tight re-packaging of sperm DNA, enabling the development of more streamlined sperm. This discovery sheds light on potential problems in sperm development and human male infertility.
Researchers identify critical gene for brain development, mental retardation
The study reveals that a specific protein, srGAP2, plays a crucial role in controlling the migration and branching of neurons during brain development. By manipulating this protein's activity, researchers were able to observe its effects on filopodia formation and neuronal behavior.
American Society for Microbiology honors Angelika Gruendling for work on lipoteichoic acids
The American Society for Microbiology has awarded Dr. Angelika Gründling the ICAAC Young Investigator Award for her groundbreaking work on lipoteichoic acids and holins in bacterial membranes. Her research revealed that holins accumulate in the membrane during infection, leading to a collapse of the potential and formation of holes.
'Disordered' amino acids may really be there to provide wiggle room for signaling protein
A study by Fox Chase Cancer Center researchers reveals that 'disordered' amino acids in the signaling protein NHERF1 enable flexibility and molecular switching. This finding challenges traditional views on the role of disordered sequences in proteins.
Heart protein regulates blood vessel maintenance
A study led by Akiko Hata of Tufts University School of Medicine found that the heart protein FHL2 regulates blood vessel maintenance. FHL2 inhibits the genes necessary for vascular smooth muscle cells to transition between a resting and proliferative state.
SourceTufts University, Health Sciences Campus·JournalJournal of Biological Chemistry·DateMay 11, 2009
Motor proteins may be vehicles for drug delivery
Researchers have discovered that motor proteins can be engineered for efficient cargo transport, potentially leading to targeted cancer treatment. By altering the function of these proteins, scientists aim to develop new drugs that inhibit kinesin activity during cell division, slowing tumor growth.
Study of protein structures reveals key events in evolutionary history
A new study of protein structures reveals a 'big bang' of innovation, coinciding with the emergence of three superkingdoms. The study constructs a timeline of protein evolution that relates directly to the history of life.
Researchers isolate protein domain linked to tumor progression
Scientists at Rensselaer Polytechnic Institute have identified a protein domain linked to tumor progression and tissue invasion. The discovery could lead to the development of targeted cancer therapies with fewer side effects.
SourceRensselaer Polytechnic Institute·JournalProceedings of the National Academy of Sciences·DateFeb 17, 2009
Scientists reveal structure of new botulism nerve toxin subtype
Researchers have determined the atomic-level structure of botulinum neurotoxin subtype E, revealing a unique arrangement that may help explain its faster-acting properties. This finding could lead to the development of faster-acting vaccines and therapeutic agents.
Redesigned protein accelerates blood clotting
Researchers have redesigned factor VIII to increase its ability to drive blood clotting, which could lead to more effective and less burdensome hemophilia treatment. The new design improves the stability of the protein, allowing it to withstand manufacturing processes and exposure to the human bloodstream.
SourceUniversity of Rochester Medical Center·JournalJournal of Thrombosis and Haemostasis·DateDec 22, 2008
Protein 'tubules' free avian flu virus from immune recognition
A protein in H5N1 avian flu virus forms tiny tubules hiding double-stranded RNA from the immune system, allowing the virus to evade an antiviral response. The discovery could lead to drug development to block this action and potentially fight influenza worldwide.
Atomic-resolution views suggest function of enzyme that regulates light-detecting signals in eye
The study provides clues about the function of phosphodiesterase 6 (PDE6) enzyme, essential to vision. PDE6 undergoes a large conformational change after binding with small messenger molecule cGMP, affecting its ability to transmit signals to the brain.
Scientists reveal the key mechanisms for affinity between transient binding proteins
Researchers at IRB Barcelona have performed the first computational analysis of transient interactions between proteins, unveiling molecular mechanisms involved in specificity. The study reveals that contextual residues determine protein recognition, with implications for drug design and cellular network resilience.
On the evolutionary trail of molecules that cause Lou Gehrig's disease
Researchers at Baylor College of Medicine have identified a key molecule linked to the progression of ALS. The protein VAPB plays a crucial role in regulating nerve-cell interactions and protein folding, with abnormal function contributing to the disease.
Carnegie Mellon scientists unveil new tool to understand evolution of multi-domain genes
Researchers have discovered a critical flaw in the standard method for analyzing gene evolution, particularly for genes encoding multi-domain proteins. A new tool called Neighborhood Correlation has been developed to correctly identify gene ancestry, which is essential for understanding gene function and regulatory circuitry. The tool ...
Census of protein architectures offers new view of history of life
Researchers compiled global census of protein architectures to plot evolution of Archaea, Bacteria, and Eukarya. The study found evidence that archaeal microbes emerged first as an evolutionarily distinguishable group, losing a fold in the process.
SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalGenome Research·DateOct 1, 2007
Chemists get grip on slippery lipids
Researchers have made significant breakthroughs in understanding how lipid binding domains interact with cell membranes to modulate functions. The study provides new targets for developing small molecules and drugs that specifically modulate signaling pathways.
Prion propagates in foreign host
Researchers have successfully propagated a prion from one organism into another, expanding our understanding of these infectious proteins and their role in fatal neurodegenerative diseases. The discovery opens up new avenues for studying prion propagation and highlights the need to search for additional prions.
Stowers Institute's Workman Lab demonstrates mechanism for decoding histone modification marks
The study reveals that a combinatorial action of multiple protein domains is required to read histone modifications, targeting the Rpd3S complex to deacetylate transcribed chromatin. This finding has significant implications for understanding and treating Huntington's disease and other neurodegenerative disorders.
Protein structures for the entire yeast proteome
Researchers predicted 3D structures for yeast proteins using de novo methods and integrated with biological data, providing a global view of protein relationships. The study assigned domains to families of evolutionarily related proteins, generating testable hypotheses about their mechanisms of action.
Research pinpoints West Nile virus antibody binding site
Purdue University researchers identified a precise location where an antibody binds to the West Nile virus and proposed a theory for its neutralization mechanism. The study suggests that this antibody works by blocking the positional changes needed for the E protein before fusion, preventing infection.
Unusual mechanism keeps repair protein accurate
Researchers at Ohio State University have discovered a novel mechanism used by the DNA repair protein, DNA polymerase lambda, to ensure accurate replication and repair of DNA. The protein utilizes an unexpected structure, known as the proline-rich domain, which is critical to its high fidelity despite initial concerns about error rates.
Prediction of a prokaryotic RNA-silencing system
Researchers identified a number of cas genes associated with CRISPR clusters, potentially involved in RNA-processing mechanisms. They propose that all CRISPR inserts are derived from viruses or plasmids, transcribed and silenced via Cas proteins.
Novel enzyme offers new look at gene regulation
A novel enzyme, JHDM1A, has been discovered to remove methyl groups from histones, a finding with diverse implications for understanding gene regulation and its role in diseases. The study suggests that many proteins containing a similar domain may also be involved in histone demethylation.
Telling axons where to go – and grow
The study reveals that Rnf6 targets LIMK1 for degradation, controlling actin dynamics and axonal growth. Changes in Rnf6 levels can be restored by compensatory changes in LIMK1 expression.
Researchers reveal secret of key protein in brain and heart function
Researchers at Brown University have solved a crucial part of the SAP97 protein's structure, allowing them to develop a molecule that can inhibit it. This breakthrough could lead to effective treatments for cardiac and neurological diseases, including learning and memory disorders and drug addiction.