1vig: Difference between revisions

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[[Image:1vig.gif|left|200px]]
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{{STRUCTURE_1vig|  PDB=1vig  |  SCENE=  }}  
{{STRUCTURE_1vig|  PDB=1vig  |  SCENE=  }}  


'''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''
===NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8612276}}


==About this Structure==
==About this Structure==
1VIG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIG OCA].  
1VIG 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=1VIG OCA].  


==Reference==
==Reference==
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[[Category: Stier, G.]]
[[Category: Stier, G.]]
[[Category: Rna-binding protein]]
[[Category: Rna-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:26:42 2008''

Revision as of 11:26, 28 July 2008

File:1vig.png

Template:STRUCTURE 1vig

NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES

Template:ABSTRACT PUBMED 8612276

About this Structure

1VIG is a Single protein structure of sequence from Homo sapiens. Full experimental 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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