1hhv
From Proteopedia
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|PDB= 1hhv |SIZE=350|CAPTION= <scene name='initialview01'>1hhv</scene> | |PDB= 1hhv |SIZE=350|CAPTION= <scene name='initialview01'>1hhv</scene> | ||
|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=1hhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhv OCA], [http://www.ebi.ac.uk/pdbsum/1hhv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hhv RCSB]</span> | ||
}} | }} | ||
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[[Category: vmip-ii]] | [[Category: vmip-ii]] | ||
| - | ''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 21:05:10 2008'' |
Revision as of 18:05, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II
Overview
Human herpesvirus-8 (HHV-8) is the infectious agent responsible for Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II (vMIP-II), which shows sequence similarity to the human CC chemokines. vMIP-II has broad receptor specificity that crosses chemokine receptor subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine receptors. In this study, the solution structure of chemically synthesized vMIP-II was determined by nuclear magnetic resonance. The protein is a monomer and possesses the chemokine fold consisting of a flexible N-terminus, three antiparallel beta strands, and a C-terminal alpha helix. Except for the N-terminal residues (residues 1-13) and the last two C-terminal residues (residues 73-74), the structure of vMIP-II is well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respectively. Taking into account the sequence differences between the various CC chemokines and comparing their three-dimensional structures allows us to implicate residues that influence the quaternary structure and receptor binding and activation of these proteins in solution. The analysis of the sequence and three-dimensional structure of vMIP-II indicates the presence of epitopes involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II was initially specific for CCR5 and acquired receptor-binding properties to CCR2 and other chemokine receptors.
About this Structure
1HHV is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure., Shao W, Fernandez E, Sachpatzidis A, Wilken J, Thompson DA, Schweitzer BI, Lolis E, Eur J Biochem. 2001 May;268(10):2948-59. PMID:11358512
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