2a55: Difference between revisions

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[[Image:2a55.gif|left|200px]]<br />

[[Image:2a55.gif|left|200px]]<br /><applet load="2a55" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2a55" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2a55" />

'''Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.'''<br />

==Overview==

Human C4b-binding protein (C4BP) protects host tissue, and those pathogens, able to hijack this plasma glycoprotein, from complement-mediated, destruction. We now show that the first two complement control protein, (CCP) modules of the C4BP alpha-chain, plus the four residues connecting, them, are necessary and sufficient for binding a bacterial virulence, factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure, determination by NMR reveals two tightly coupled CCP modules in an, elongated arrangement within this region of C4BP. Chemical shift, perturbation studies demonstrate that the N-terminal, hypervariable region, of M4 binds to a site including strand 1 of CCP module 2. This interaction, is accompanied by an intermodular reorientation within C4BP. We thus, provide a detailed picture of an interaction whereby a pathogen evades, complement.

Human C4b-binding protein (C4BP) protects host tissue, and those pathogens able to hijack this plasma glycoprotein, from complement-mediated destruction. We now show that the first two complement control protein (CCP) modules of the C4BP alpha-chain, plus the four residues connecting them, are necessary and sufficient for binding a bacterial virulence factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure determination by NMR reveals two tightly coupled CCP modules in an elongated arrangement within this region of C4BP. Chemical shift perturbation studies demonstrate that the N-terminal, hypervariable region of M4 binds to a site including strand 1 of CCP module 2. This interaction is accompanied by an intermodular reorientation within C4BP. We thus provide a detailed picture of an interaction whereby a pathogen evades complement.

==About this Structure==

2A55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2A55 OCA].

2A55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A55 OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Ball, G.]]

[[Category: Barlow, P.N.]]

[[Category: Barlow, P N.]]

[[Category: Blom, A.M.]]

[[Category: Blom, A M.]]

[[Category: Jenkins, H.T.]]

[[Category: Jenkins, H T.]]

[[Category: Lindahl, G.]]

[[Category: Mark, L.]]

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[[Category: scr]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:46:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:42 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2a55.gif|left|200px]]<br />
+[[Image:2a55.gif|left|200px]]<br /><applet load="2a55" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2a55" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2a55" />
 '''Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.'''<br />
 ==Overview==
-Human C4b-binding protein (C4BP) protects host tissue, and those pathogens, able to hijack this plasma glycoprotein, from complement-mediated, destruction. We now show that the first two complement control protein, (CCP) modules of the C4BP alpha-chain, plus the four residues connecting, them, are necessary and sufficient for binding a bacterial virulence, factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure, determination by NMR reveals two tightly coupled CCP modules in an, elongated arrangement within this region of C4BP. Chemical shift, perturbation studies demonstrate that the N-terminal, hypervariable region, of M4 binds to a site including strand 1 of CCP module 2. This interaction, is accompanied by an intermodular reorientation within C4BP. We thus, provide a detailed picture of an interaction whereby a pathogen evades, complement.
+Human C4b-binding protein (C4BP) protects host tissue, and those pathogens able to hijack this plasma glycoprotein, from complement-mediated destruction. We now show that the first two complement control protein (CCP) modules of the C4BP alpha-chain, plus the four residues connecting them, are necessary and sufficient for binding a bacterial virulence factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure determination by NMR reveals two tightly coupled CCP modules in an elongated arrangement within this region of C4BP. Chemical shift perturbation studies demonstrate that the N-terminal, hypervariable region of M4 binds to a site including strand 1 of CCP module 2. This interaction is accompanied by an intermodular reorientation within C4BP. We thus provide a detailed picture of an interaction whereby a pathogen evades complement.
 ==About this Structure==
-A55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A55 OCA].
+A55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A55 OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Ball, G.]]
-[[Category: Barlow, P.N.]]
+[[Category: Barlow, P N.]]
-[[Category: Blom, A.M.]]
+[[Category: Blom, A M.]]
-[[Category: Jenkins, H.T.]]
+[[Category: Jenkins, H T.]]
 [[Category: Lindahl, G.]]
 [[Category: Mark, L.]]
@@ Line 25: / Line 24: @@
 [[Category: scr]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:46:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:42 2008''