1cm9
From Proteopedia
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| - | [[Image:1cm9.gif|left|200px]] | + | [[Image:1cm9.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II''' | + | {{Structure |
| + | |PDB= 1cm9 |SIZE=350|CAPTION= <scene name='initialview01'>1cm9</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CM9 is a [ | + | 1CM9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11041848 11041848] |
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: karposi's sarcoma]] | [[Category: karposi's sarcoma]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:08 2008'' |
Revision as of 08:26, 20 March 2008
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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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