2gox
From Proteopedia
(New page: 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: C3 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120700 120700]], Macular degeneration, age-related, 9 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120700 120700]] | ||
==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'' |
Revision as of 11:31, 23 January 2008
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Crystal structure of Efb-C / C3d Complex
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.
About this Structure
2GOX is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
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):430-437. Epub 2007 Mar 11. PMID:17351618
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