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1hfg

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(New page: 200px<br /><applet load="1hfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hfg" /> '''NMR SOLUTION STRUCTURE OF VMIP-II 1-71 FROM ...)
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[[Image:1hfg.gif|left|200px]]<br /><applet load="1hfg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hfg" />
 
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'''NMR SOLUTION STRUCTURE OF VMIP-II 1-71 FROM KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS (MINIMIZED AVERAGE STRUCTURE).'''<br />
 
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==Overview==
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==NMR solution structure of vMIP-II 1-71 from Kaposi's sarcoma-associated herpesvirus (minimized average structure).==
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Kaposi's sarcoma-associated herpesvirus encodes a chemokine called vMIP-II, that has been shown to be a broad range human chemokine receptor, antagonist. Two N-terminal peptides, vMIP-II(1-10) and vMIP-II(1-11)dimer, (dimerised through Cys11) were synthesised. Both peptides are shown to, bind the CXC chemokine receptor 4 (CXCR4). vMIP-II(1-10) was 1400-fold, less potent than the native protein whilst the vMIP-II(1-11)dimer was only, 180-fold less potent. In addition, both peptides are CXCR4 antagonists., Through analysis of non-standard, long mixing time two-dimensional nuclear, Overhauser enhancement spectroscopy experiments, 13C relaxation data and, amide chemical shift temperature gradients for the N-terminus of vMIP-II, we show that this region populates a turn-like structure over residues, 5-8, both in the presence and absence of the full protein scaffold. This, major conformation is likely to be in fast exchange with other, conformational states but it has not previously been detected in monomeric, chemokine structures. This and other studies [Elisseeva et al. (2000) J., Biol. Chem. 275, 26799-26805] suggest that there may be a link between the, structuring of the short N-terminal chemokine peptides and their ability, to bind their receptor.
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<StructureSection load='1hfg' size='340' side='right'caption='[[1hfg]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hfg]] 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=1HFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFG FirstGlance]. <br>
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1HFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFG OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfg OCA], [https://pdbe.org/1hfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfg RCSB], [https://www.ebi.ac.uk/pdbsum/1hfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfg ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structure/function of human herpesvirus-8 MIP-II (1-71) and the antagonist N-terminal segment (1-10)., Crump MP, Elisseeva E, Gong J, Clark-Lewis I, Sykes BD, FEBS Lett. 2001 Feb 2;489(2-3):171-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11165244 11165244]
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== Function ==
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[[Category: Human herpesvirus 4]]
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[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.
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Clark-Lewis, I.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Crump, M.P.]]
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Check<jmol>
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[[Category: Elisseeva, E.]]
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<jmolCheckbox>
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[[Category: Gong, J.H.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/1hfg_consurf.spt"</scriptWhenChecked>
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[[Category: Sykes, B.D.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: anatagonist]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: chemokine]]
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</jmolCheckbox>
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[[Category: cxcr4]]
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</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=1hfg ConSurf].
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[[Category: vmip-ii]]
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<div style="clear:both"></div>
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__TOC__
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:34:11 2007''
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</StructureSection>
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[[Category: Human gammaherpesvirus 8]]
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[[Category: Large Structures]]
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[[Category: Clark-Lewis I]]
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[[Category: Crump MP]]
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[[Category: Elisseeva E]]
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[[Category: Gong J-H]]
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[[Category: Sykes BD]]

Current revision

NMR solution structure of vMIP-II 1-71 from Kaposi's sarcoma-associated herpesvirus (minimized average structure).

PDB ID 1hfg

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