1cm9

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[[Image:1cm9.gif|left|200px]]
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{{Structure
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|PDB= 1cm9 |SIZE=350|CAPTION= <scene name='initialview01'>1cm9</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1cm9", creates the "Structure Box" on the page.
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{{STRUCTURE_1cm9| PDB=1cm9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm9 OCA], [http://www.ebi.ac.uk/pdbsum/1cm9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cm9 RCSB]</span>
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'''CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II'''
'''CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II'''
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[[Category: Fernandez, E J.]]
[[Category: Fernandez, E J.]]
[[Category: Lolis, E.]]
[[Category: Lolis, E.]]
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[[Category: chemokine]]
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[[Category: Chemokine]]
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[[Category: herpesvirus-8]]
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[[Category: Herpesvirus-8]]
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[[Category: karposi's sarcoma]]
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[[Category: Karposi's sarcoma]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:53:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:22 2008''
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Revision as of 09:53, 2 May 2008

Template:STRUCTURE 1cm9

CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II


Overview

Herpesvirus-8 macrophage inflammatory protein-II (vMIP-II) binds a uniquely wide spectrum of chemokine receptors. We report the X-ray structure of vMIP-II determined to 2.1 A resolution. Like RANTES, vMIP-II crystallizes as a dimer and displays the conventional chemokine tertiary fold. We have compared the surface topology and electrostatic potential of vMIP-II to those of eotaxin-1, RANTES, and MCP-3, three CCR3 physiological agonists with known three-dimensional structures. Surface epitopes identified on RANTES to be involved in binding to CCR3 are mimicked on the eotaxin-1 and MCP-3 surface. However, the surface topology of vMIP-II in these regions is markedly different. The results presented here indicate that the structural basis for interaction with the chemokine receptor CCR3 by vMIP-II is different from that for the physiological agonists eotaxin-1, RANTES, and MCP-3. These differences on vMIP-II may be a consequence of its broad-range receptor recognition capabilities.

About this Structure

1CM9 is a Single protein structure of sequence from Human herpesvirus 8. Full crystallographic information is available from OCA.

Reference

Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation., Fernandez EJ, Wilken J, Thompson DA, Peiper SC, Lolis E, Biochemistry. 2000 Oct 24;39(42):12837-44. PMID:11041848 Page seeded by OCA on Fri May 2 12:53:09 2008

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