View source for 1vih


==NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE==
<StructureSection load='1vih' size='340' side='right'caption='[[1vih]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vih]] 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=1VIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1vih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vih OCA], [https://pdbe.org/1vih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vih RCSB], [https://www.ebi.ac.uk/pdbsum/1vih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vih ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/vi/1vih_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1vih ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vih" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gibson TJ]]
[[Category: Joseph C]]
[[Category: Morelli MAC]]
[[Category: Musco G]]
[[Category: Nilges M]]
[[Category: Pastore A]]
[[Category: Stier G]]