4bl4 | pdb_00004bl4

Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.

spinqualitylabelsall models 4bl4, resolution 4.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bl4 is a 4 chain structure with sequence from Borreliella burgdorferi ZS7. This structure supersedes the now removed PDB entry 4atr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4.06Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3BZN5_BORBZ Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Complement Regulator-Acquiring Surface Protein Complement regulator-acquiring surface protein

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