1g44: Difference between revisions

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New page: left|200px<br /><applet load="1g44" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g44, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1g44.jpg|left|200px]]<br /><applet load="1g44" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g44.jpg|left|200px]]<br /><applet load="1g44" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g44, resolution 2.6&Aring;" />
caption="1g44, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF A COMPLEMENT CONTROL PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS'''<br />
'''CRYSTAL STRUCTURE OF A COMPLEMENT CONTROL PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS'''<br />


==Overview==
==Overview==
Vaccinia virus complement control protein (VCP) inhibits both pathways of, complement activation through binding the third and fourth components. A, homolog of mammalian regulators of complement activation, its ability to, bind heparin endows VCP with additional activities of significance to, viral infectivity. The structure of VCP reveals a highly extended molecule, with a putative heparin recognition site at its C-terminal end. A second, cluster of positive charges provides a possibly overlapping binding site, for both heparin and complement components. Experiments suggested by the, structure indicate that VCP can bind heparin and control complement, simultaneously. This, the structure of any intact regulator of complement, activation, along with attendant functional insights, will stimulate the, design of new therapeutic inhibitors of complement.
Vaccinia virus complement control protein (VCP) inhibits both pathways of complement activation through binding the third and fourth components. A homolog of mammalian regulators of complement activation, its ability to bind heparin endows VCP with additional activities of significance to viral infectivity. The structure of VCP reveals a highly extended molecule with a putative heparin recognition site at its C-terminal end. A second cluster of positive charges provides a possibly overlapping binding site for both heparin and complement components. Experiments suggested by the structure indicate that VCP can bind heparin and control complement simultaneously. This, the structure of any intact regulator of complement activation, along with attendant functional insights, will stimulate the design of new therapeutic inhibitors of complement.


==About this Structure==
==About this Structure==
1G44 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G44 OCA].  
1G44 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G44 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
[[Category: Barlow, P.N.]]
[[Category: Barlow, P N.]]
[[Category: Ganesh, V.K.]]
[[Category: Ganesh, V K.]]
[[Category: Judge, K.W.]]
[[Category: Judge, K W.]]
[[Category: Kotwal, G.J.]]
[[Category: Kotwal, G J.]]
[[Category: Mullin, N.]]
[[Category: Mullin, N.]]
[[Category: Murthy, K.H.M.]]
[[Category: Murthy, K H.M.]]
[[Category: Ogata, C.M.]]
[[Category: Ogata, C M.]]
[[Category: Smith, S.A.]]
[[Category: Smith, S A.]]
[[Category: beta]]
[[Category: beta]]
[[Category: module]]
[[Category: module]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:41:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:00 2008''

Revision as of 13:46, 21 February 2008

File:1g44.jpg


1g44, resolution 2.6Å

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CRYSTAL STRUCTURE OF A COMPLEMENT CONTROL PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS

OverviewOverview

Vaccinia virus complement control protein (VCP) inhibits both pathways of complement activation through binding the third and fourth components. A homolog of mammalian regulators of complement activation, its ability to bind heparin endows VCP with additional activities of significance to viral infectivity. The structure of VCP reveals a highly extended molecule with a putative heparin recognition site at its C-terminal end. A second cluster of positive charges provides a possibly overlapping binding site for both heparin and complement components. Experiments suggested by the structure indicate that VCP can bind heparin and control complement simultaneously. This, the structure of any intact regulator of complement activation, along with attendant functional insights, will stimulate the design of new therapeutic inhibitors of complement.

About this StructureAbout this Structure

1G44 is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans., Murthy KH, Smith SA, Ganesh VK, Judge KW, Mullin N, Barlow PN, Ogata CM, Kotwal GJ, Cell. 2001 Jan 26;104(2):301-11. PMID:11207370

Page seeded by OCA on Thu Feb 21 12:46:00 2008

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OCA, Eric Martz