1vig

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[[Image:1vig.gif|left|200px]]
 
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==NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1vig", creates the "Structure Box" on the page.
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<StructureSection load='1vig' size='340' side='right'caption='[[1vig]]' 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'>[[1vig]] 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=1VIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIG 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</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=1vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vig OCA], [https://pdbe.org/1vig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vig RCSB], [https://www.ebi.ac.uk/pdbsum/1vig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vig ProSAT]</span></td></tr>
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{{STRUCTURE_1vig| PDB=1vig | SCENE= }}
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</table>
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== Function ==
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'''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''
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[https://www.uniprot.org/uniprot/VIGLN_HUMAN VIGLN_HUMAN] Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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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/vi/1vig_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=1vig 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 ==
The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.
The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.
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==About this Structure==
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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome.,Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A Cell. 1996 Apr 19;85(2):237-45. PMID:8612276<ref>PMID:8612276</ref>
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1VIG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome., Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A, Cell. 1996 Apr 19;85(2):237-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8612276 8612276]
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</div>
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<div class="pdbe-citations 1vig" style="background-color:#fffaf0;"></div>
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== References ==
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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: Gibson, T J.]]
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[[Category: Gibson TJ]]
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[[Category: Joseph, C.]]
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[[Category: Joseph C]]
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[[Category: Morelli, M A.C.]]
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[[Category: Morelli MAC]]
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[[Category: Musco, G.]]
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[[Category: Musco G]]
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[[Category: Nilges, M.]]
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[[Category: Nilges M]]
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[[Category: Pastore, A.]]
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[[Category: Pastore A]]
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[[Category: Stier, G.]]
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[[Category: Stier G]]
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[[Category: Rna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:34:05 2008''
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Current revision

NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES

PDB ID 1vig

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