Biophysical Reviews

, Volume 5, Issue 1, pp 29–39

SH3 domains: modules of protein–protein interactions

Authors

    • Department of Biophysics, The School of Theoretical Modeling
  • Udayan Guha
    • Medical Oncology Branch, National Cancer InstituteNational Institutes of Health
Review

DOI: 10.1007/s12551-012-0081-z

Cite this article as:
Kurochkina, N. & Guha, U. Biophys Rev (2013) 5: 29. doi:10.1007/s12551-012-0081-z

Abstract

Src homology 3 (SH3) domains are involved in the regulation of important cellular pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of polyproline and a number of noncanonical sequences by SH3 domains has been extensively studied by crystallography, nuclear magnetic resonance and other methods. High-affinity peptides that bind SH3 domains are used in drug development as candidates for anticancer treatment. This review summarizes the latest achievements in deciphering structural determinants of SH3 function.

Keywords

Three-dimensional structureSH3 domainCell signalingSrc-familyMyosinProtein conformation

Abbreviations

Ack-1

Activated CDC42-associated kinase

Csk

Carboxyl-terminal Src kinase

Fyn

FGR and yes-related novel kinase

Hck

Hematopoetic cell kinase

IB1

Islet brain 1

PEP

Proline-enriched phosphatase

PEST

Proline/glutamic acid/serine/threonine-rich domain

PTK

Protein tyrosine kinase

SH3

Src homology 3

Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer 2012