Snake venom metalloproteases--structure and function of catalytic and disintegrin domains

Comp Biochem Physiol C Toxicol Pharmacol. 2006 Mar-Apr;142(3-4):328-346. doi: 10.1016/j.cbpc.2005.11.005. Epub 2006 Jan 24.

Abstract

Snake venoms are relevant sources of toxins that have evolved towards the engineering of highly active compounds. In the last years, research efforts have produced great advance in their understanding and uses. Metalloproteases with disintegrin domains are among the most abundant toxins in many Viperidae snake venoms. This review will focus on the structure, function and possible applications of the metalloprotease and disintegrin domains.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Disintegrins / chemistry*
  • Disintegrins / metabolism
  • Humans
  • Metalloproteases / chemistry*
  • Metalloproteases / metabolism
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Snake Venoms / enzymology*
  • Snakes

Substances

  • Disintegrins
  • Snake Venoms
  • Metalloproteases