2gom

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gom OCA], [https://pdbe.org/2gom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gom RCSB], [https://www.ebi.ac.uk/pdbsum/2gom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gom ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

To provide insight into bacterial suppression of complement-mediated immunity, we present here structures of a bacterial complement inhibitory protein, both free and bound to its complement target. The 1.25-A structure of the complement component C3-inhibitory domain of Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C) demonstrated a helical motif involved in complement regulation, whereas the 2.2-A structure of Efb-C bound to the C3d domain of human C3 allowed insight into the recognition of complement proteins by invading pathogens. Our structure-function studies provided evidence for a previously unrecognized mode of complement inhibition whereby Efb-C binds to native C3 and alters the solution conformation of C3 in a way that renders it unable to participate in successful 'downstream' activation of the complement response.

A structural basis for complement inhibition by Staphylococcus aureus.,Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD, Geisbrecht BV Nat Immunol. 2007 Apr;8(4):430-7. Epub 2007 Mar 11. PMID:17351618<ref>PMID:17351618</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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