1cm9
From Proteopedia
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|PDB= 1cm9 |SIZE=350|CAPTION= <scene name='initialview01'>1cm9</scene>, resolution 2.1Å | |PDB= 1cm9 |SIZE=350|CAPTION= <scene name='initialview01'>1cm9</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==About this Structure== | ==About this Structure== | ||
| - | 1CM9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1CM9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. 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://www.ncbi.nlm.nih.gov/pubmed/11041848 11041848] | 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 | + | [[Category: Human herpesvirus 8]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fernandez, E J.]] | [[Category: Fernandez, E J.]] | ||
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[[Category: karposi's sarcoma]] | [[Category: karposi's sarcoma]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:22 2008'' |
Revision as of 16:24, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 19:24:22 2008
