Title | Protein-protein interaction through beta-strand addition. |
Publication Type | Journal Article |
Year of Publication | 2006 |
Authors | Remaut, H., and G. Waksman |
Journal | Trends Biochem Sci |
Volume | 31 |
Issue | 8 |
Pagination | 436-44 |
Date Published | 2006 Aug |
ISSN | 0968-0004 |
Keywords | Animals, 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. |
DOI | 10.1016/j.tibs.2006.06.007 |
Alternate Journal | Trends Biochem. Sci. |
PubMed ID | 16828554 |
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