Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca

Imagem de Miniatura




Watanabe, L.
Vieira, D. F.
Bortoleto, R. K.
Arni, R. K.

Título da Revista

ISSN da Revista

Título de Volume


Blackwell Munksgaard


Bothrombin, a snake-venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non-crosslinked soft clots, aggregates platelets in the presence of exogeneous fibrinogen and activates blood coagulation factor VIII. Bothrombin shares high sequence homology with other snake-venom proteases such as batroxobin (94% identity), but only 30 and 34% identity with human alpha-thrombin and trypsin, respectively. Single crystals of bothrombin have been obtained and X-ray diffraction data have been collected at the Laboratorio Nacional de Luz Sincrotron to a resolution of 2.8 Angstrom. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 94.81, b = 115.68, c = 155.97 Angstrom.



Como citar

Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1036-1038, 2002.