Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca
Carregando...
Fontes externas
Fontes externas
Data
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
Blackwell Munksgaard
International Union of Crystallography (IUCr)
International Union of Crystallography (IUCr)
Tipo
Artigo
Direito de acesso
Acesso aberto
Fontes externas
Fontes externas
Resumo
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.
Descrição
Palavras-chave
Idioma
Inglês
Citação
Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 58, p. 1036-1038, 2002.
