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Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.
Structural highlights
FunctionPublication Abstract from PubMedBorrelia 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. Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi.,Caesar JJ, Wallich R, Kraiczy P, Zipfel PF, Lea SM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):629-33. doi: , 10.1107/S1744309113012748. Epub 2013 May 23. PMID:23722839[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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