Relative solvent accessible surface area predicts protein conformational changes upon binding

Joseph A Marsh, Sarah A Teichmann

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Protein interactions are often accompanied by significant changes in conformation. We have analyzed the relationships between protein structures and the conformational changes they undergo upon binding. Based upon this, we introduce a simple measure, the relative solvent accessible surface area, which can be used to predict the magnitude of binding-induced conformational changes from the structures of either monomeric proteins or bound subunits. Applying this to a large set of protein complexes suggests that large conformational changes upon binding are common. In addition, we observe considerable enrichment of intrinsically disordered sequences in proteins predicted to undergo large conformational changes. Finally, we demonstrate that the relative solvent accessible surface area of monomeric proteins can be used as a simple proxy for protein flexibility. This reveals a powerful connection between the flexibility of unbound proteins and their binding-induced conformational changes, consistent with the conformational selection model of molecular recognition.
Original languageEnglish
Pages (from-to)859-67
Number of pages9
JournalStructure
Volume19
Issue number6
DOIs
Publication statusPublished - 8 Jun 2011

Keywords / Materials (for Non-textual outputs)

  • Models, Molecular
  • Multiprotein Complexes
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Proteins
  • Solvents
  • Surface Properties
  • Water

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