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  Structural and biochemical analysis on Ras-effector signaling via RalGDS

Vetter, I. R., Linnemann, T., Wohlgemuth, S., Geyer, M., Kalbitzer, H. R., Herrmann, C., et al. (1999). Structural and biochemical analysis on Ras-effector signaling via RalGDS. FEBS Letters, 451(2), 175-180. doi:10.1016/S0014-5793(99)00555-4.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-5BB9-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-5BBA-A
Genre: Journal Article
Alternative Title : Structural and biochemical analysis on Ras-effector signaling via RalGDS

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FEBSLett_451_1999_175.pdf (Any fulltext), 837KB
 
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 Creators:
Vetter, Ingrid R., Author
Linnemann, Thomas, Author
Wohlgemuth, Sabine, Author
Geyer, Matthias1, Author              
Kalbitzer, Hans Robert1, Author              
Herrmann, Christian, Author
Wittinghofer, Alfred1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Ras; Ras-binding domain; Structure; RalGDS; Signaling
 Abstract: The structure of the complex of Ras with the Ras-binding domain of its effector RalGDS (RGS-RBD), the first genuine Ras-effector complex, has been solved by X-ray crystallography. As with the Rap-RafRBD complex (Nasser et al., 1995), the interaction is via an inter-protein β-sheet between the switch I region of Ras and the second strand of the RGS-RBD sheet, but the details of the interactions in the interface are remarkably different. Mutational studies were performed to investigate the contribution of selected interface residues to the binding affinity. Gel filtration experiments show that the Ras·RGS-RBD complex is a monomer. The results are compared to a recently determined structure of a similar complex using a Ras mutant (Huang et al., 1998) and are discussed in relation to partial loss-of-function mutations and the specificity of Ras versus Rap binding

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Language(s): eng - English
 Dates: 1999-04-081999-02-251999-04-081999-05-21
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 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: 451 (2) Sequence Number: - Start / End Page: 175 - 180 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501