1hhv: Difference between revisions
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[[Image:1hhv.gif|left|200px]] | [[Image:1hhv.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II''' | {{Structure | ||
|PDB= 1hhv |SIZE=350|CAPTION= <scene name='initialview01'>1hhv</scene> | |||
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|LIGAND= | |||
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'''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HHV is a [ | 1HHV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11358512 11358512] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fernandez, E.]] | [[Category: Fernandez, E.]] | ||
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[[Category: vmip-ii]] | [[Category: vmip-ii]] | ||
''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 11:37:20 2008'' | ||
Revision as of 09:37, 20 March 2008
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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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