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  The KH module has an αβ fold

Castiglione Morelli, M. A., Stier, G., Gibson, T. J., Joseph, C., Musco, G., Pastore, A., et al. (1995). The KH module has an αβ fold. FEBS Letters, 358(2), 193-198. doi:10.1016/0014-5793(94)01422-W.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A80E-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AEB8-E
Genre: Journal Article
Alternative Title : The KH module has an alpha beta fold

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FEBSLett_358_1995_193.pdf (Any fulltext), 459KB
 
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 Creators:
Castiglione Morelli, Maria Antonietta, Author
Stier, Gunter1, Author              
Gibson, Toby J., Author
Joseph, Catherine, Author
Musco, Giovanna, Author
Pastore, Annalisa, Author
Travè, Gilles, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: KH; Module; Vigilin; Structure; NMR; 1D, 2D and 3D, One-, two- and three-dimensional; HSQC; heteronuclear single quantum coherence; NMR; nuclear magnetic resonance; NOE; nuclear Overhauser enhancement; NOESY, 2D NOE spectroscopy; TPPI; time-proportional phase incrementation; TOCSY; total correlation spectroscopy
 Abstract: The KH module has recently been identified in a number of RNA associated proteins including vigilin and FMR1, a protein implicated in the fragile X syndrome. In this work, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin). Almost complete assignments were obtained for the 1H and 15N resonances using uniform 15N-labeling of the protein combined with homo-nuclear 2D 1HNMR and 3D 15N correlated 1H NMR. On the basis of NOE patterns, secondary chemical shifts and amide solvent exposure, the secondary structure consists of an antiparallel three stranded beta sheet connected by two helical regions. This domain may also be stabilized by an appended C-terminal helix which is common to many but not all members of the KH family.

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Language(s): eng - English
 Dates: 1994-11-281994-12-142000-02-231995-01-23
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664776
DOI: 10.1016/0014-5793(94)01422-W
URI: https://www.ncbi.nlm.nih.gov/pubmed/7828735
Other: 7347
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 358 (2) Sequence Number: - Start / End Page: 193 - 198 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501