A model for fibrinogen: domains and sequence.
Science
; 230(4732): 1388-91, 1985 Dec 20.
Article
em En
| MEDLINE
| ID: mdl-4071058
ABSTRACT
Electron microscopy of rotary-shadowed fibrinogen demonstrates that the molecules modified for crystallization by limited cleavage with a bacterial protease retain the major features of the native structure. This evidence, together with image processing and x-ray analysis of the crystals and of fibrin, has been used to develop a three-dimensional low resolution model for the molecule. The data indicate that the two large end domains of the molecule would be composed of the carboxyl-terminus of the B beta chain (proximal) and gamma chain (distal), respectively; the carboxyl-terminus of the A alpha chain would fold back to form an additional central domain. On this basis, the carboxyl-terminal region of each of the three chains of fibrinogen is folded independently into a globular domain.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fibrinogênio
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Science
Ano de publicação:
1985
Tipo de documento:
Article