Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions

Siyuan Ren, Vladimir N. Uversky, Zhengjun Chen, A. Dunker, Zoran Obradovic

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Background: 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.

Original languageEnglish
Article numberS26
JournalBMC Genomics
Volume9
Issue numberSUPPL. 2
DOIs
StatePublished - Sep 16 2008

Fingerprint

Phosphotransferases
Proteins
Signal Transduction
Amino Acids

ASJC Scopus subject areas

  • Biotechnology
  • Genetics

Cite this

Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions. / Ren, Siyuan; Uversky, Vladimir N.; Chen, Zhengjun; Dunker, A.; Obradovic, Zoran.

In: BMC Genomics, Vol. 9, No. SUPPL. 2, S26, 16.09.2008.

Research output: Contribution to journalArticle

Ren, Siyuan ; Uversky, Vladimir N. ; Chen, Zhengjun ; Dunker, A. ; Obradovic, Zoran. / Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions. In: BMC Genomics. 2008 ; Vol. 9, No. SUPPL. 2.
@article{b0b659e1cb6e4ffa987ebdea7d71a8a7,
title = "Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions",
abstract = "Background: 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.",
author = "Siyuan Ren and Uversky, {Vladimir N.} and Zhengjun Chen and A. Dunker and Zoran Obradovic",
year = "2008",
month = "9",
day = "16",
doi = "10.1186/1471-2164-9-S2-S26",
language = "English",
volume = "9",
journal = "BMC Genomics",
issn = "1471-2164",
publisher = "BioMed Central",
number = "SUPPL. 2",

}

TY - JOUR

T1 - Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions

AU - Ren, Siyuan

AU - Uversky, Vladimir N.

AU - Chen, Zhengjun

AU - Dunker, A.

AU - Obradovic, Zoran

PY - 2008/9/16

Y1 - 2008/9/16

N2 - Background: 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.

AB - Background: 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.

UR - http://www.scopus.com/inward/record.url?scp=52249101769&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=52249101769&partnerID=8YFLogxK

U2 - 10.1186/1471-2164-9-S2-S26

DO - 10.1186/1471-2164-9-S2-S26

M3 - Article

VL - 9

JO - BMC Genomics

JF - BMC Genomics

SN - 1471-2164

IS - SUPPL. 2

M1 - S26

ER -