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1cq3

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(New page: 200px<br /><applet load="1cq3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq3, resolution 1.85&Aring;" /> '''STRUCTURE OF A SOLUB...)
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[[Image:1cq3.jpg|left|200px]]<br /><applet load="1cq3" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cq3.jpg|left|200px]]<br /><applet load="1cq3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1cq3, resolution 1.85&Aring;" />
caption="1cq3, resolution 1.85&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CQ3 OCA].
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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.]]
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[[Category: Smith, C.A.]]
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[[Category: Smith, C A.]]
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[[Category: Smolak, P.J.]]
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[[Category: Smolak, P J.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: beta sandwich]]
[[Category: beta sandwich]]
[[Category: chemokine]]
[[Category: chemokine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:48:16 2007''
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''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


1cq3, resolution 1.85Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 12:08:34 2008

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