2gom: Difference between revisions

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==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==

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==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17351618 17351618]

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: Single protein]]

[[Category: Staphylococcus aureus]]

[[Category: Geisbrecht, B.V.]]

[[Category: Geisbrecht, B V.]]

[[Category: Hammel, M.]]

[[Category: three-helix closed bundle with left-hand twist]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:45 2008''

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 10: / Line 10: @@
 ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17351618 17351618]
+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: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Geisbrecht, B.V.]]
+[[Category: Geisbrecht, B V.]]
 [[Category: Hammel, M.]]
 [[Category: three-helix closed bundle with left-hand twist]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:36:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:45 2008''