Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases.
The importance of proteinases in the pathologies associated with Viperid envenoming has long been appreciated. Over the past 40 years substantial research has clearly implicated metalloproteinases in the venom (snake venom metalloproteinases; SVMPs) as playing key roles in the development of such symptoms as hemorrhage, edema, hypotension, hypovolemia, inflammation and necrosis. In spite of this wealth of information there are still many unresolved questions pertaining to the structural basis for the various SVMPS giving rise to the diversity of activities. In this short review we will not attempt to provide an exhaustive collation of structural studies on the SVMPs; however, we will give a brief outline of the structural classification of the SVMPs; as well as relate them to the other members of the reprolysin family of metalloproteinases, the ADAMs. The information put forth in the text does not allow specific conclusions to be drawn on the structural basis for SVMP functional diversity, but it is our goal that it will allow for the development of testable hypotheses that can be experimentally pursued. What the reader will observe is that there are very interesting structural features displayed by the various SVMP classes and subclasses that provide insight into their functional characteristics.
Fox
Jay W
JW
Department of Microbiology, Health Sciences Center, University of Virginia, Charlottesville, VA 22908-0734, USA. jwf8x@virginia.edu
Serrano
Solange M T
SM
D000595:Amino Acid Sequence; D000818:Animals; D019483:Disintegrins / Q000235:genetics*; D040461:Gene Components; D045726:Metalloproteases / Q000145:classification / Q000235:genetics*; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D012910:Snake Venoms / Q000201:enzymology* / Q000235:genetics; D012911:Snakes / Q000235:genetics*
D019483:Disintegrins; D012910:Snake Venoms; D045726:Metalloproteases