title: Structure, function and evolutionary relationship of proteins containing a disintegrin domain.
abstract: Disintegrins are soluble integrin ligands from snake venoms that disrupt cell-matrix interactions. Recently, the nuclear magnetic resonance structures of two disintegrins were determined, providing provocative molecular insight into how a disintegrin may engage an integrin. In addition, it has recently been realized that disintegrins are derived from larger multifunctional proteins, and that there is a family of membrane-anchored, disintegrin domain-containing proteins that may promote important cell-cell interactions.
authors.affiliation: Department of Pharmacology, University of California, San Francisco 94143-0450.
authors.forename: C P
authors.initials: CP
authors.lastname: Blobel
authors.forename: J M
authors.initials: JM
authors.lastname: White
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002448:Cell Adhesion; D019483:Disintegrins; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D008969:Molecular Sequence Data; D009842:Oligopeptides; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D010975:Platelet Aggregation Inhibitors; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D014688:Venoms / Q000737:chemistry / Q000494:pharmacology
chemical_list: D019483:Disintegrins; D008565:Membrane Proteins; D009842:Oligopeptides; D010455:Peptides; D010975:Platelet Aggregation Inhibitors; D011506:Proteins; D014688:Venoms; C047981:arginyl-glycyl-aspartic acid