View source for 1vmp


==STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II==
<StructureSection load='1vmp' size='340' side='right'caption='[[1vmp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_8 Human gammaherpesvirus 8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VMP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vmp OCA], [https://pdbe.org/1vmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vmp RCSB], [https://www.ebi.ac.uk/pdbsum/1vmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vmp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VMI2_HHV8P VMI2_HHV8P] Blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors. May form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/1vmp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vmp ConSurf].
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== Publication Abstract from PubMed ==
We report the solution structure of the chemotactic cytokine (chemokine) vMIP-II. This protein has unique biological activities in that it blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors, some of which are used by HJV to gain cell entry. vMIP-II is a monomeric protein, unlike most members of the chemokine family, and its structure consists of a disordered N-terminus, followed by a helical turn (Gln25-Leu27), which leads into the first strand of a three-stranded antiparallel beta-sheet (Ser29-Thr34; Gly42-Thr47; Gln52-Asp56). Following the sheet is a C-terminal alpha-helix, which extends from residue Asp60 until Gln68. The final five residues beyond the C-terminal helix (Pro70-Arg74) are in an extended conformation, but several of these C-terminal residues contact the first beta-strand. The structure of vMIP-II is compared to other chemokines that also block infection by HIV-1, and the structural basis of its lack of ability to form a dimer is discussed.

The solution structure of the anti-HIV chemokine vMIP-II.,Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ Protein Sci. 1999 Nov;8(11):2270-80. PMID:10595530<ref>PMID:10595530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human gammaherpesvirus 8]]
[[Category: Large Structures]]
[[Category: Liwang AC]]
[[Category: Liwang PJ]]
[[Category: Peiper SC]]
[[Category: Sun Y]]
[[Category: Wang Z-X]]