2gox: Difference between revisions
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New page: left|200px<br /> <applet load="2gox" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gox, resolution 2.200Å" /> '''Crystal structure ... |
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[[Image:2gox. | [[Image:2gox.jpg|left|200px]]<br /><applet load="2gox" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2gox" size=" | |||
caption="2gox, resolution 2.200Å" /> | caption="2gox, resolution 2.200Å" /> | ||
'''Crystal structure of Efb-C / C3d Complex'''<br /> | '''Crystal structure of Efb-C / C3d Complex'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
2GOX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http:// | 2GOX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:31:53 2008'' | ||
