1vig
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(New page: 200px<br /> <applet load="1vig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vig" /> '''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTUR...)
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Revision as of 17:37, 12 November 2007
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NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES
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
1VIG 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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