Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.
J Mol Biol
; 392(3): 787-802, 2009 Sep 25.
Article
em En
| MEDLINE
| ID: mdl-19631658
ABSTRACT
Collagens contain a unique triple-helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization, and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Estrutura Terciária de Proteína
/
Estrutura Quaternária de Proteína
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Colágeno Tipo XVIII
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Multimerização Proteica
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Estados Unidos