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| - | [[Image:1hhv.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hhv| PDB=1hhv | SCENE= }} | | {{STRUCTURE_1hhv| PDB=1hhv | SCENE= }} |
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| - | '''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II'''
| + | ===SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11358512}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11358512 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11358512}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1HHV is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA]. | + | 1HHV is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Virus chemokine]] | | [[Category: Virus chemokine]] |
| | [[Category: Vmip-ii]] | | [[Category: Vmip-ii]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:51:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:12:16 2008'' |
Revision as of 05:12, 1 July 2008
Template:STRUCTURE 1hhv
SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II
Template:ABSTRACT PUBMED 11358512
About this Structure
1HHV is a Single protein structure. Full experimental 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
Page seeded by OCA on Tue Jul 1 08:12:16 2008
