Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 6): 629-33, 2013 Jun.
Article
em En
| MEDLINE
| ID: mdl-23722839
ABSTRACT
Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Fator H do Complemento
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Borrelia burgdorferi
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article