Modular peptide recognition domains in eukaryotic signaling

John Kuriyan, David Cowburn

Research output: Contribution to journalArticle

446 Citations (Scopus)

Abstract

A characteristic feature of cellular signal transduction pathways in eukaryotes is the separation of catalysis from target recognition. Several modular domains that recognize short peptide sequences and target signaling proteins to these sequences have been identified. The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and these results are reviewed here. In addition, the mechanism of cooperative interactions between these domains is discussed.

Original languageEnglish (US)
Pages (from-to)259-288
Number of pages30
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume26
DOIs
StatePublished - 1997
Externally publishedYes

Fingerprint

Signal transduction
src Homology Domains
X ray crystallography
X Ray Crystallography
Eukaryota
Catalysis
Peptides
Signal Transduction
Nuclear magnetic resonance
Proteins
Protein Domains

Keywords

  • PDZ
  • PTB
  • SH2
  • SH3
  • Src homology
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

Modular peptide recognition domains in eukaryotic signaling. / Kuriyan, John; Cowburn, David.

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 26, 1997, p. 259-288.

Research output: Contribution to journalArticle

@article{33673892aaaa44b48054d043b8cda7a7,
title = "Modular peptide recognition domains in eukaryotic signaling",
abstract = "A characteristic feature of cellular signal transduction pathways in eukaryotes is the separation of catalysis from target recognition. Several modular domains that recognize short peptide sequences and target signaling proteins to these sequences have been identified. The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and these results are reviewed here. In addition, the mechanism of cooperative interactions between these domains is discussed.",
keywords = "PDZ, PTB, SH2, SH3, Src homology, Tyrosine kinase",
author = "John Kuriyan and David Cowburn",
year = "1997",
doi = "10.1146/annurev.biophys.26.1.259",
language = "English (US)",
volume = "26",
pages = "259--288",
journal = "Annual Review of Biophysics",
issn = "1936-122X",
publisher = "Annual Reviews Inc.",

}

TY - JOUR

T1 - Modular peptide recognition domains in eukaryotic signaling

AU - Kuriyan, John

AU - Cowburn, David

PY - 1997

Y1 - 1997

N2 - A characteristic feature of cellular signal transduction pathways in eukaryotes is the separation of catalysis from target recognition. Several modular domains that recognize short peptide sequences and target signaling proteins to these sequences have been identified. The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and these results are reviewed here. In addition, the mechanism of cooperative interactions between these domains is discussed.

AB - A characteristic feature of cellular signal transduction pathways in eukaryotes is the separation of catalysis from target recognition. Several modular domains that recognize short peptide sequences and target signaling proteins to these sequences have been identified. The structural bases of the specificities of recognition by SH2, SH3, and PTB domains have been elucidated by X-ray crystallography and NMR, and these results are reviewed here. In addition, the mechanism of cooperative interactions between these domains is discussed.

KW - PDZ

KW - PTB

KW - SH2

KW - SH3

KW - Src homology

KW - Tyrosine kinase

UR - http://www.scopus.com/inward/record.url?scp=0030950608&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030950608&partnerID=8YFLogxK

U2 - 10.1146/annurev.biophys.26.1.259

DO - 10.1146/annurev.biophys.26.1.259

M3 - Article

C2 - 9241420

AN - SCOPUS:0030950608

VL - 26

SP - 259

EP - 288

JO - Annual Review of Biophysics

JF - Annual Review of Biophysics

SN - 1936-122X

ER -