Luxury accommodations: the expanding role of structural plasticity in protein-protein interactions

Structure. 2000 Jul 15;8(7):R137-42. doi: 10.1016/s0969-2126(00)00167-2.

Abstract

The recognition of multiple ligands at a single molecular surface is essential to many biological processes. Conformational flexibility has emerged as a compelling strategy for association at such convergent binding sites. Studies over the past few years have brought about a greater understanding of the role that protein plasticity might play in protein-protein interactions.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigens / metabolism
  • Binding Sites*
  • Consensus Sequence
  • Crystallography, X-Ray
  • Erythropoietin / agonists
  • Erythropoietin / metabolism
  • Histocompatibility Antigens Class I / metabolism
  • Humans
  • Immunoglobulin Fc Fragments / chemistry
  • Immunoglobulin Fc Fragments / metabolism
  • Ligands
  • Models, Molecular
  • Peptide Library
  • Protein Binding*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proteins / genetics
  • Proteins / metabolism
  • Receptors, Antigen, T-Cell / chemistry
  • Receptors, Antigen, T-Cell / metabolism
  • Receptors, Erythropoietin / chemistry
  • Receptors, Erythropoietin / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Antigens
  • Histocompatibility Antigens Class I
  • Immunoglobulin Fc Fragments
  • Ligands
  • Peptide Library
  • Proteins
  • Receptors, Antigen, T-Cell
  • Receptors, Erythropoietin
  • Erythropoietin