7b26 | pdb_00007b26

CirpA1 in complex with pseudo-monomeric Properdin lacking TSR2-3

spinqualitylabelsall models 7b26, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b26 is a 3 chain structure with sequence from Homo sapiens and Rhipicephalus pulchellus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: BGC, BMA, FUC, MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease PROP_HUMAN Defects in CFP are the cause of properdin deficiency (PFD) [MIM:312060. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III). Function PROP_HUMAN A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. Publication Abstract from PubMed Activation of the serum-resident complement system begins a cascade that leads to activation of membrane-resident complement receptors on immune cells, thus coordinating serum and cellular immune responses. Whilst many molecules act to control inappropriate activation, Properdin is the only known positive regulator of the human complement system. By stabilising the alternative pathway C3 convertase it promotes complement self-amplification and persistent activation boosting the magnitude of the serum complement response by all triggers. In this work, we identify a family of tick-derived alternative pathway complement inhibitors, hereafter termed CirpA. Functional and structural characterisation reveals that members of the CirpA family directly bind to properdin, inhibiting its ability to promote complement activation, and leading to potent inhibition of the complement response in a species specific manner. We provide a full functional and structural characterisation of a properdin inhibitor, opening avenues for future therapeutic approaches. Structure and function of a family of tick-derived complement inhibitors targeting properdin.,Braunger K, Ahn J, Jore MM, Johnson S, Tang TTL, Pedersen DV, Andersen GR, Lea SM Nat Commun. 2022 Jan 14;13(1):317. doi: 10.1038/s41467-021-27920-2. PMID:35031611 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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