Snake venom metalloproteases--structure and function of catalytic and disintegrin domains.
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.
Ramos
O H P
OHP
Departamento de Ciências Fisiológicas, Universidade Federal de São Carlos, Rodovia Washington Luis, Km 235, São Carlos, SP, 13565-905, Brazil.
Selistre-de-Araujo
H S
HS
Departamento de Ciências Fisiológicas, Universidade Federal de São Carlos, Rodovia Washington Luis, Km 235, São Carlos, SP, 13565-905, Brazil. Electronic address: hsaraujo@power.ufscar.br.
D000595:Amino Acid Sequence; D000818:Animals; D019483:Disintegrins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D045726:Metalloproteases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012910:Snake Venoms / Q000201:enzymology*; D012911:Snakes
D019483:Disintegrins; D012910:Snake Venoms; D045726:Metalloproteases