Viper venom disintegrins and related molecules.
The term "disintegrin" was first used in 1990 to describe a group of viper venom-derived, nonenzymatic small proteins that shared numerous structural and functional properties. These proteins, which have been found in a great number of viper species studied since that time possess both a remarkable sequence homology and an equally notable variability in potency and selectivity in their interactions with integrin receptors. The discovery that small disintegrins may actually have been derived from much larger mosaic proteins possessing catalytic activity, and that species other than snakes (both plant and animal) produce proteins containing disintegrin-like domains, has led to much research related to both the proteins themselves and the receptors to which they bind. The purpose of this review is to discuss the literature and the authors' own data on the structure and function of disintegrins and their relevance to the studies on proteins containing disintegrin-like domains, such as hemorrhagins and ADAMs.
McLane
M A
MA
Department of Medical Technology, University of Delaware, Newark 19716, USA.
Marcinkiewicz
C
C
Vijay-Kumar
S
S
Wierzbicka-Patynowski
I
I
Niewiarowski
S
S
D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D019483:Disintegrins / Q000737:chemistry / Q000378:metabolism; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D014757:Viper Venoms
D019483:Disintegrins; D010975:Platelet Aggregation Inhibitors; D014757:Viper Venoms; D010450:Endopeptidases; C041605:hemorrhagic proteinase IV