title: The molecular architecture of protein-protein binding sites.
abstract: The formation of specific protein interactions plays a crucial role in most, if not all, biological processes, including signal transduction, cell regulation, the immune response and others. Recent advances in our understanding of the molecular architecture of protein-protein binding sites, which facilitates such diversity in binding affinity and specificity, are enabling us to address key questions. What is the amino acid composition of binding sites? What are interface hotspots? How are binding sites organized? What are the differences between tight and weak interacting complexes? How does water contribute to binding? Can the knowledge gained be translated into protein design? And does a universal code for binding exist, or is it the architecture and chemistry of the interface that enable diverse but specific binding solutions?
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Dana
authors.initials: D
authors.lastname: Reichmann
authors.forename: Ofer
authors.initials: O
authors.lastname: Rahat
authors.forename: Mati
authors.initials: M
authors.lastname: Cohen
authors.forename: Hani
authors.initials: H
authors.lastname: Neuvirth
authors.forename: Gideon
authors.initials: G
authors.lastname: Schreiber
mesh_terms: D001665:Binding Sites; D046912:Multiprotein Complexes; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D014867:Water / Q000737:chemistry
chemical_list: D046912:Multiprotein Complexes; D011506:Proteins; D014867:Water