1cm9
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(New page: 200px<br /><applet load="1cm9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cm9, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 10:27, 20 November 2007
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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 4. 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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