Structural insight into binding of Staphylococcus aureus to human fibronectin.
FEBS Lett
; 580(1): 273-7, 2006 Jan 09.
Article
em En
| MEDLINE
| ID: mdl-16376343
ABSTRACT
Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and alignment of beta-strands that are predicted to bind the peptide. The module pair is elongated, as in the unbound state. Combined with evidence that residues in both 4F1 and 5F1 are directly involved in peptide binding, this observation supports the hypothesis that, when bound to intact Fn, the bacterial protein adopts an unusual, highly extended conformation.
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Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Staphylococcus aureus
/
Fibronectinas
/
Adesinas Bacterianas
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Reino Unido