1y7x

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(New page: 200px<br /> <applet load="1y7x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y7x" /> '''Solution structure of a two-repeat fragment...)
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[[Image:1y7x.gif|left|200px]]<br />
 
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<applet load="1y7x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1y7x" />
 
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'''Solution structure of a two-repeat fragment of major vault protein'''<br />
 
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==Overview==
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==Solution structure of a two-repeat fragment of major vault protein==
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Major vault protein (MVP) is the main constituent of vaults, large, ribonucleoprotein particles implicated in resistance to cancer therapy and, correlated with poor survival prognosis. Here, we report the structure of, the main repeat element in human MVP. The approximately 55 amino acid, residue MVP domain has a unique, novel fold that consists of a, three-stranded antiparallel beta-sheet. The solution NMR structure of a, two-domain fragment reveals the interdomain contacts and relative, orientations of the two MVP domains. We use these results to model the, assembly of 672 MVP domains from 96 MVP molecules into the ribs of the, 13MDa vault structure. The unique features include a thin, skin-like, structure with polar residues on both the cytoplasmic and internal, surface, and a pole-to-pole arrangement of MVP molecules. These studies, provide a starting point for understanding the self-assembly of MVP into, vaults and their interactions with other proteins. Chemical shift, perturbation studies identified the binding site of vault poly(ADP-ribose), polymerase, another component of vault particles, indicating that MVP, domains form a new class of interaction-mediating modules.
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<StructureSection load='1y7x' size='340' side='right'caption='[[1y7x]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1y7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y7X FirstGlance]. <br>
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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=1y7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y7x OCA], [https://pdbe.org/1y7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y7x RCSB], [https://www.ebi.ac.uk/pdbsum/1y7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y7x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MVP_HUMAN MVP_HUMAN] Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases.<ref>PMID:15133037</ref> <ref>PMID:16441665</ref> <ref>PMID:16418217</ref>
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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/y7/1y7x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1y7x 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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Major vault protein (MVP) is the main constituent of vaults, large ribonucleoprotein particles implicated in resistance to cancer therapy and correlated with poor survival prognosis. Here, we report the structure of the main repeat element in human MVP. The approximately 55 amino acid residue MVP domain has a unique, novel fold that consists of a three-stranded antiparallel beta-sheet. The solution NMR structure of a two-domain fragment reveals the interdomain contacts and relative orientations of the two MVP domains. We use these results to model the assembly of 672 MVP domains from 96 MVP molecules into the ribs of the 13MDa vault structure. The unique features include a thin, skin-like structure with polar residues on both the cytoplasmic and internal surface, and a pole-to-pole arrangement of MVP molecules. These studies provide a starting point for understanding the self-assembly of MVP into vaults and their interactions with other proteins. Chemical shift perturbation studies identified the binding site of vault poly(ADP-ribose) polymerase, another component of vault particles, indicating that MVP domains form a new class of interaction-mediating modules.
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==Disease==
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Solution structure of a two-repeat fragment of major vault protein.,Kozlov G, Vavelyuk O, Minailiuc O, Banville D, Gehring K, Ekiel I J Mol Biol. 2006 Feb 17;356(2):444-52. Epub 2005 Dec 7. PMID:16373071<ref>PMID:16373071</ref>
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Known diseases associated with this structure: Leigh syndrome, French-Canadian type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607544 607544]], Mitral valve prolapse, myxomatous 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=157700 157700]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1Y7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y7X OCA].
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</div>
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<div class="pdbe-citations 1y7x" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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Solution structure of a two-repeat fragment of major vault protein., Kozlov G, Vavelyuk O, Minailiuc O, Banville D, Gehring K, Ekiel I, J Mol Biol. 2006 Feb 17;356(2):444-52. Epub 2005 Dec 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16373071 16373071]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Banville, D.]]
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[[Category: Banville D]]
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[[Category: Ekiel, I.]]
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[[Category: Ekiel I]]
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[[Category: Gehring, K.]]
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[[Category: Gehring K]]
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[[Category: Kozlov, G.]]
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[[Category: Kozlov G]]
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[[Category: Minailiuc, O.]]
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[[Category: Minailiuc O]]
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[[Category: Vavelyuk, O.]]
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[[Category: Vavelyuk O]]
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[[Category: beta-sheet modules]]
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[[Category: structural repeats]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:15:57 2007''
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Current revision

Solution structure of a two-repeat fragment of major vault protein

PDB ID 1y7x

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