1vig
From Proteopedia
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'''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES''' | '''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES''' | ||
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[[Category: Pastore, A.]] | [[Category: Pastore, A.]] | ||
[[Category: Stier, G.]] | [[Category: Stier, G.]] | ||
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Revision as of 09:34, 3 May 2008
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 Page seeded by OCA on Sat May 3 12:34:05 2008
