1hfg

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{{Seed}}
 
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[[Image:1hfg.png|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_1hfg", creates the "Structure Box" on the page.
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<StructureSection load='1hfg' size='340' side='right'caption='[[1hfg]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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, 1 model</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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{{STRUCTURE_1hfg| PDB=1hfg | SCENE= }}
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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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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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===NMR SOLUTION STRUCTURE OF VMIP-II 1-71 FROM KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS (MINIMIZED AVERAGE STRUCTURE).===
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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:11165244<ref>PMID:11165244</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11165244}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1hfg" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11165244 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11165244}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human gammaherpesvirus 8]]
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1HFG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFG OCA].
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[[Category: Large Structures]]
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[[Category: Clark-Lewis I]]
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==Reference==
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[[Category: Crump MP]]
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<ref group="xtra">PMID:11165244</ref><references group="xtra"/>
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[[Category: Elisseeva E]]
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[[Category: Human herpesvirus 8]]
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[[Category: Gong J-H]]
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[[Category: Clark-Lewis, I.]]
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[[Category: Sykes BD]]
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[[Category: Crump, M P.]]
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[[Category: Elisseeva, E.]]
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[[Category: Gong, J H.]]
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[[Category: Sykes, B D.]]
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[[Category: Anatagonist]]
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[[Category: Chemokine]]
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[[Category: Cxcr4]]
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[[Category: Vmip-ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:24:18 2009''
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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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