Modular Protein Domains

  • ID: 2179556
  • Book
  • 524 Pages
  • John Wiley and Sons Ltd
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The definitive reference on protein modules covers all relevant modular domains mediating protein–protein interactions:

– SH2, SH3, WW domains

– EVH1 and GYF domains

– PTB and FHA domains

– Protein kinase domains

– SET, Bromo and Chromo domains

– PDZ and EH domains

– Ubiquitin– and actin–binding domains

– Phosphoinositide–binding domains

Structure, function and interaction partners of the domains are systematically treated, a general section covers methods to study protein–protein interactions on a proteome–wide scale.

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INTRODUCTION

An overview of protein to protein interactions and protein modules

SH2 domain as a paradigm of protein modules

PROTEIN BINDING DOMAINS THAT INTERACT WITH PROLINE LIGANDS

SH3 domain

WW domain

EVH1 domain

GYF domain

PROTEIN BINDING DOMAINS AND THEIR REGULATION BY PHOSPHORYLATION

PTB domain

FHA domains

14–3–3 proteins and phospho–serine/theronine binding modules

Protein kinase domains as important catalytic domains functionally linked to protein binding domains

PROTEIN DOMAINS REGULATING CHROMATIN FUNCTION

SET domains

Bromo domain

Chromo & Shadow–Chromo domains

PROTEIN DOMAINS RECOGNIZING SHORT PEPTIDE CORES IN THEIR LIGANDS

PDZ domain

EH domain

EXAMPLES OF FUNCTIONAL DIVERSITY AMONG PROTEIN DOMAINS: UBIQUITIN AND ACTIN BINDING DOMAINS

Ubiquitin–Binding Domains

CH domain

PHOSPHO–INOSITIDE BINDING PROTEIN DOMAINS

PH domain

VHS and ENTH domains

PX domain

DISSECTING DOMAINS AND LIGANDS WITH PEPTIDE CHEMISTRY AND COMPUTERS

Peptide and protein repertoires for global analysis of modules

Computational analysis of modular protein domains

Nomenclatures for protein modules and their cognate motifs

EPILOGUE: Future perspectives

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"... the book is well written and provides clear, concise and informative reviews on some of the most common domains involved in protein–peptide interactions."

Nature Cell Biology, July 2005

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