1vih

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:25, 9 May 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1vih.png|left|200px]]
 
-
<!--
+
==NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE==
-
The line below this paragraph, containing "STRUCTURE_1vih", creates the "Structure Box" on the page.
+
<StructureSection load='1vih' size='340' side='right'caption='[[1vih]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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>
-
{{STRUCTURE_1vih| PDB=1vih | SCENE= }}
+
</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.
-
===NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE===
+
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>
-
The line below this paragraph, {{ABSTRACT_PUBMED_8612276}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1vih" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 8612276 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_8612276}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1VIH is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==Reference==
+
-
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]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Gibson, T J.]]
+
[[Category: Gibson TJ]]
-
[[Category: Joseph, C.]]
+
[[Category: Joseph C]]
-
[[Category: Morelli, M A.C.]]
+
[[Category: Morelli MAC]]
-
[[Category: Musco, G.]]
+
[[Category: Musco G]]
-
[[Category: Nilges, M.]]
+
[[Category: Nilges M]]
-
[[Category: Pastore, A.]]
+
[[Category: Pastore A]]
-
[[Category: Stier, G.]]
+
[[Category: Stier G]]
-
[[Category: Rna-binding protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:42:36 2008''
+

Current revision

NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE

PDB ID 1vih

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vih"
Personal tools