Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom of Bothrops jararaca.
Bothrombin, a snake-venom serine protease, specifically cleaves fibrinogen, releasing fibrinopeptide A to form non-crosslinked soft clots, aggregates platelets in the presence of exogenous 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 A. 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 A.
Watanabe
L
L
Department of Physics, IBILCE/UNESP, CP 136, Sao José do Rio Preto, CEP 15054-000, Brazil.
Vieira
D F
DF
Bortoleto
R K
RK
Arni
R K
RK
D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry* / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005340:Fibrinogen / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry*
D003435:Crotalid Venoms; D005340:Fibrinogen; D012697:Serine Endopeptidases; C086027:bothrombin