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dc.creatorRen, S
dc.creatorUversky, VN
dc.creatorChen, Z
dc.creatorDunker, AK
dc.creatorObradovic, Z
dc.date.accessioned2021-02-01T21:54:00Z
dc.date.available2021-02-01T21:54:00Z
dc.date.issued2008-09-16
dc.identifier.issn1471-2164
dc.identifier.issn1471-2164
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5583
dc.identifier.other18831792 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5601
dc.description.abstractBackground: Protein interactions are essential for most cellular functions. Interactions mediated by domains that appear in a large number of proteins are of particular interest since they are expected to have an impact on diversities of cellular processes such as signal transduction and immune response. Many well represented domains recognize and bind to primary sequences less than 10 amino acids in length called Short Linear Motifs (SLiMs). Results: In this study, we systematically studied the evolutionary conservation of SLiMs recognized by SH2, SH3 and Ser/Thr Kinase domains in both ordered and disordered protein regions. Disordered protein regions are protein sequences that lack a fixed three-dimensional structure under putatively native conditions. We find that, in all these domains examined, SLiMs are more conserved in disordered regions. This trend is more evident in those protein functional groups that are frequently reported to interact with specific domains. Conclusion: The correlation between SLiM conservation with disorder prediction demonstrates that functional SLiMs recognized by each domain occur more often in disordered as compared to structured regions of proteins. © 2008 Ren et al; licensee BioMed Central Ltd.
dc.format.extentS26-S26
dc.language.isoen
dc.relation.haspartBMC Genomics
dc.relation.isreferencedbySpringer Science and Business Media LLC
dc.rightsCC BY
dc.subjectAmino Acid Motifs
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBinding Sites
dc.subjectComputational Biology
dc.subjectConserved Sequence
dc.subjectDatabases, Protein
dc.subjectHumans
dc.subjectProtein-Serine-Threonine Kinases
dc.subjectProteins
dc.subjectSequence Analysis, Protein
dc.subjectSequence Homology, Amino Acid
dc.subjectStructure-Activity Relationship
dc.subjectsrc Homology Domains
dc.titleShort Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions
dc.typeArticle
dc.type.genreConference Proceeding
dc.relation.doi10.1186/1471-2164-9-S2-S26
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.date.updated2021-02-01T21:53:57Z
refterms.dateFOA2021-02-01T21:54:00Z


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