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  Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome

Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M. A., Nilges, M., Gibson, T. J., et al. (1996). Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85(2), 237-245. doi:10.1016/S0092-8674(00)81100-9.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A6DD-C Version Permalink: http://hdl.handle.net/21.11116/0000-0004-41F8-B
Genre: Journal Article

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Cell_85_1996_237.pdf (Any fulltext), 3MB
 
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 Creators:
Musco, Giovanna, Author
Stier, Gunter1, Author              
Joseph, Catherine, Author
Castiglione Morelli, Maria Antonietta, Author
Nilges, Michael, Author
Gibson, Toby J., Author
Pastore, Annalisa, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: 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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Language(s): eng - English
 Dates: 1995-11-081996-02-062000-10-031996-04-19
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664778
DOI: 10.1016/S0092-8674(00)81100-9
URI: https://www.ncbi.nlm.nih.gov/pubmed/8612276
Other: 7345
 Degree: -

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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 85 (2) Sequence Number: - Start / End Page: 237 - 245 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183