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Verfasst von:Caesar, Joseph J. E. [VerfasserIn]   i
 Wallich, Reinhard [VerfasserIn]   i
 Kraiczy, Peter [VerfasserIn]   i
 Zipfel, Peter F. [VerfasserIn]   i
 Lea, Susan M. [VerfasserIn]   i
Titel:Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi
Verf.angabe:Joseph J.E. Caesar, Reinhard Wallich, Peter Kraiczy, Peter F. Zipfel and Susan M. Lea
E-Jahr:2013
Jahr:9 May 2013
Umfang:5 S.
Fussnoten:Gesehen am 28.01.2021
Titel Quelle:Enthalten in: Acta crystallographica / F
Ort Quelle:Oxford [u.a.] : Blackwell, 2005
Jahr Quelle:2013
Band/Heft Quelle:69(2013), 6, Seite 629-633
ISSN Quelle:2053-230X
 1744-3091
Abstract:B. burgdorferi binds complement factor H using a dimeric surface protein, CspA (BbCRASP-1). Presented here is a new structure of CspA that suggests that there is a degree of flexibility between subunits which may have implications for complement regulator binding., - 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.
DOI:doi:10.1107/S1744309113012748
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1107/S1744309113012748
 Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668580/
 DOI: https://doi.org/10.1107/S1744309113012748
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1745938672
Verknüpfungen:→ Zeitschrift

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