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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biophysik     Display Documents



ID: 565688.0, MPI für medizinische Forschung / Abteilung Biophysik
Structural and biochemical analysis on Ras−effector signaling via RalGDS
Translation of Title:Structural and biochemical analysis on Ras−effector signaling via RalGDS
Authors:Vetter, Ingrid R.; Linnemann, Thomas; Wohlgemuth, Sabine; Geyer, Matthias; Kalbitzer, Hans Robert; Herrmann, Christian; Wittinghofer, Alfred
Language:English
Date of Publication (YYYY-MM-DD):1999-05-21
Title of Journal:FEBS Letters
Journal Abbrev.:FEBS Lett.
Volume:451
Issue / Number:2
Start Page:175
End Page:180
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Free Keywords:Ras; Ras−binding domain; Structure; RalGDS; Signaling
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
Identifiers:LOCALID:4487
URI:http%3A%2F%2Fwww.sciencedirect.com%2Fscience%3F_ob...
URI:http%3A%2F%2Fdx.doi.org%2F10.1016%2FS0014-5793%289...
URI:http%3A%2F%2Fwww.mendeley.com%2Fresearch%2Fstructu...
DOI:10.1016%2FS0014-5793%2899%2900555-4
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