1cq3
From Proteopedia
(New page: 200px<br /><applet load="1cq3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq3, resolution 1.85Å" /> '''STRUCTURE OF A SOLUB...) |
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- | [[Image:1cq3.jpg|left|200px]]<br /><applet load="1cq3" size=" | + | [[Image:1cq3.jpg|left|200px]]<br /><applet load="1cq3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cq3, resolution 1.85Å" /> | caption="1cq3, resolution 1.85Å" /> | ||
'''STRUCTURE OF A SOLUBLE SECRETED CHEMOKINE INHIBITOR, VCCI, FROM COWPOX VIRUS'''<br /> | '''STRUCTURE OF A SOLUBLE SECRETED CHEMOKINE INHIBITOR, VCCI, FROM COWPOX VIRUS'''<br /> | ||
==Overview== | ==Overview== | ||
- | Most poxviruses, including variola, the causative agent of smallpox, express a secreted protein of 35 kDa, vCCI, which binds CC-chemokines with | + | Most poxviruses, including variola, the causative agent of smallpox, express a secreted protein of 35 kDa, vCCI, which binds CC-chemokines with high affinity. This viral protein competes with the host cellular CC-chemokine receptors (CCRs), reducing inflammation and interfering with the host immune response. Such proteins or derivatives may have therapeutic uses as anti-inflammatory agents. We have determined the crystal structure to 1.85-A resolution of vCCI from cowpox virus, the prototype of this poxvirus virulence factor. The molecule is a beta-sandwich of topology not previously described. A patch of conserved residues on the exposed face of a beta-sheet that is strongly negatively charged might have a role in binding of CC-chemokines, which are positively charged. |
==About this Structure== | ==About this Structure== | ||
- | 1CQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupixi_virus Cupixi virus]. Full crystallographic information is available from [http:// | + | 1CQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupixi_virus Cupixi virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Carfi, A.]] | [[Category: Carfi, A.]] | ||
[[Category: McGrew, J.]] | [[Category: McGrew, J.]] | ||
- | [[Category: Smith, C | + | [[Category: Smith, C A.]] |
- | [[Category: Smolak, P | + | [[Category: Smolak, P J.]] |
- | [[Category: Wiley, D | + | [[Category: Wiley, D C.]] |
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: chemokine]] | [[Category: chemokine]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:34 2008'' |
Revision as of 10:08, 21 February 2008
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STRUCTURE OF A SOLUBLE SECRETED CHEMOKINE INHIBITOR, VCCI, FROM COWPOX VIRUS
Overview
Most poxviruses, including variola, the causative agent of smallpox, express a secreted protein of 35 kDa, vCCI, which binds CC-chemokines with high affinity. This viral protein competes with the host cellular CC-chemokine receptors (CCRs), reducing inflammation and interfering with the host immune response. Such proteins or derivatives may have therapeutic uses as anti-inflammatory agents. We have determined the crystal structure to 1.85-A resolution of vCCI from cowpox virus, the prototype of this poxvirus virulence factor. The molecule is a beta-sandwich of topology not previously described. A patch of conserved residues on the exposed face of a beta-sheet that is strongly negatively charged might have a role in binding of CC-chemokines, which are positively charged.
About this Structure
1CQ3 is a Single protein structure of sequence from Cupixi virus. Full crystallographic information is available from OCA.
Reference
Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus., Carfi A, Smith CA, Smolak PJ, McGrew J, Wiley DC, Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12379-83. PMID:10535930
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