4BL4
Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.
Replaces: 4ATRSummary for 4BL4
Entry DOI | 10.2210/pdb4bl4/pdb |
Descriptor | COMPLEMENT REGULATOR-ACQUIRING SURFACE PROTEIN 1 (CRASP-1) (1 entity in total) |
Functional Keywords | protein binding |
Biological source | BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE) |
Total number of polymer chains | 4 |
Total formula weight | 85914.37 |
Authors | Caesar, J.J.E.,Wallich, R.,Kraiczy, P.,Zipfel, P.F.,Lea, S.M. (deposition date: 2013-05-01, release date: 2013-06-05, Last modification date: 2023-12-20) |
Primary citation | Caesar, J.J.E.,Wallich, R.,Kraiczy, P.,Zipfel, P.F.,Lea, S.M. 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, 69:629-, 2013 Cited by PubMed 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. PubMed: 23722839DOI: 10.1107/S1744309113012748 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.06 Å) |
Structure validation
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