1cm9

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{{STRUCTURE_1cm9| PDB=1cm9 | SCENE= }}
{{STRUCTURE_1cm9| PDB=1cm9 | SCENE= }}
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'''CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II'''
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===CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11041848 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11041848}}
==About this Structure==
==About this Structure==
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[[Category: Herpesvirus-8]]
[[Category: Herpesvirus-8]]
[[Category: Karposi's sarcoma]]
[[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 Mon Jun 30 20:56:34 2008''

Revision as of 17:56, 30 June 2008

Image:1cm9.png

Template:STRUCTURE 1cm9

CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II

Template:ABSTRACT PUBMED 11041848

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

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