2gox

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==Overview==
==Overview==
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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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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==
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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==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17351618 17351618]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17351618 17351618]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Geisbrecht, B.V.]]
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[[Category: Geisbrecht, B V.]]
[[Category: Hammel, M.]]
[[Category: Hammel, M.]]
[[Category: cell adhesion/toxin complex]]
[[Category: cell adhesion/toxin complex]]
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:31:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:48 2008''

Revision as of 15:33, 21 February 2008


2gox, resolution 2.200Å

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Crystal structure of Efb-C / C3d Complex

Contents

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.

Disease

Known diseases associated with this structure: C3 deficiency OMIM:[120700], Macular degeneration, age-related, 9 OMIM:[120700]

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):430-7. Epub 2007 Mar 11. PMID:17351618

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