1vih

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|ACTIVITY=
|ACTIVITY=
|GENE= HUMAN VIGILIN SIXTH KH REPEAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= HUMAN VIGILIN SIXTH KH REPEAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=[[1vig|1VIG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vih OCA], [http://www.ebi.ac.uk/pdbsum/1vih PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vih RCSB]</span>
}}
}}
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[[Category: rna-binding protein]]
[[Category: rna-binding protein]]
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Revision as of 21:25, 30 March 2008


PDB ID 1vih

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Gene: HUMAN VIGILIN SIXTH KH REPEAT (Homo sapiens)
Related: 1VIG


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE


Overview

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.

About this Structure

1VIH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from 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:8612276

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