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
Date Published2006 Aug
KeywordsAnimals, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Folding, Protein Structure, Secondary, Proteins

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.

Alternate JournalTrends Biochem. Sci.
PubMed ID16828554