Protein-protein interaction through beta-strand addition.

TitleProtein-protein interaction through beta-strand addition.
Publication TypeJournal Article
Year of Publication2006
AuthorsRemaut, H., and G. Waksman
JournalTrends Biochem Sci
Volume31
Issue8
Pagination436-44
Date Published2006 Aug
ISSN0968-0004
KeywordsAnimals, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Folding, Protein Structure, Secondary, Proteins
Abstract

Protein-protein interactions have essential roles at almost every level of organization and communication in living cells. During complex formation, proteins can interact via covalent, surface-surface or peptide-surface contacts. Many protein complexes are now known to involve the binding of linear motifs in one of the binding partners. An emerging mechanism of such non-covalent peptide-surface interaction involves the donation or addition of a beta strand in the ligand to a beta sheet or a beta strand in the receptor. Such 'beta-strand addition' contacts can dictate or modulate binding specificity and affinity, or can be used in more promiscuous protein-protein contacts. Three main classes of beta-strand addition can be distinguished: beta-sheet augmentation; beta-strand insertion and fold complementation; and beta-strand zippering. A survey of protein-protein complexes in the protein data bank identifies beta-strand additions in many important metabolic pathways. Targeting these interactions might, thus, provide novel routes for rational drug design.

DOI10.1016/j.tibs.2006.06.007
Alternate JournalTrends Biochem. Sci.
PubMed ID16828554