1vig
From Proteopedia
(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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caption="1vig" /> | caption="1vig" /> | ||
'''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''<br /> | '''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The KH module is a sequence motif found in a number of proteins that are | + | 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== | ==About this Structure== | ||
| - | 1VIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1VIG is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gibson, T | + | [[Category: Gibson, T J.]] |
[[Category: Joseph, C.]] | [[Category: Joseph, C.]] | ||
| - | [[Category: Morelli, M | + | [[Category: Morelli, M A.C.]] |
[[Category: Musco, G.]] | [[Category: Musco, G.]] | ||
[[Category: Nilges, M.]] | [[Category: Nilges, M.]] | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:39 2008'' |
Revision as of 13:35, 21 February 2008
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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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