ArticleNucleic acids research2010
ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Unified access to up-to-date residue-level annotations from UniProtKB and other biological databases for PDB data.Scientific data · 2023Article
- AHoJ: rapid, tailored search and retrieval of apo and holo protein structures for user-defined ligands.Bioinformatics (Oxford, England) · 2022Article
- D3PM: a comprehensive database for protein motions ranging from residue to domain.BMC bioinformatics · 2022Article
- CCProf: exploring conformational change profile of proteins.Database : the journal of biological databases and curation · 2016Article
- Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.Journal of the American Society for Mass Spectrometry · 2015Article
- Protein flexibility in the light of structural alphabets.Frontiers in molecular biosciences · 2015Review
- Amino Acids in Nine Ligand-Prefer Ramachandran Regions.BioMed research international · 2015Article
- IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners.Nucleic acids research · 2014Article
- Structural interface parameters are discriminatory in recognising near-native poses of protein-protein interactions.PloS one · 2014Article
- Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators.Frontiers in molecular biosciences · 2014Review
- An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.Journal of biomolecular structure & dynamics · 2013Article
- Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes.Molecular bioSystems · 2013Article
- Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins.BMC structural biology · 2012Article
- Structure fluctuations and conformational changes in protein binding.Journal of bioinformatics and computational biology · 2012Article
- AH-DB: collecting protein structure pairs before and after binding.Nucleic acids research · 2012Article
- Intrinsic protein disorder in human pathways.Molecular bioSystems · 2012Article
- Expanding the proteome: disordered and alternatively folded proteins.Quarterly reviews of biophysics · 2011Article
- CSpritz: accurate prediction of protein disorder segments with annotation for homology, secondary structure and linear motifs.Nucleic acids research · 2011Article
- Disordered patterns in clustered Protein Data Bank and in eukaryotic and bacterial proteomes.PloS one · 2011Article
- Intrinsic disorder and protein multibinding in domain, terminal, and linker regions.Molecular bioSystems · 2010Article
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6 authors.
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Abstract
Most of the proteins in a cell assemble into complexes to carry out their function. In this work, we have created a new database (named ComSin) of protein structures in bound (complex) and unbound (single) states to provide a researcher with exhaustive information on structures of the same or homologous proteins in bound and unbound states. From the complete Protein Data Bank (PDB), we selected 24 910 pairs of protein structures in bound and unbound states, and identified regions of intrinsic disorder. For 2448 pairs, the proteins in bound and unbound states are identical, while 7129 pairs have sequence identity 90% or larger. The developed server enables one to search for proteins in bound and unbound states with several options including sequence similarity between the corresponding proteins in bound and unbound states, and validation of interaction interfaces of protein complexes. Besides that, through our web server, one can obtain necessary information for studying disorder-to-order and order-to-disorder transitions upon complex formation, and analyze structural differences between proteins in bound and unbound states. The database is available at http://antares.protres.ru/comsin/.
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