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Structural and biochemical analysis of Ras-effector signaling via RalGDS

Vetter, I. R. and Linnemann, T. and Wohlgemuth, S. and Geyer, M. and Kalbitzer, Hans Robert and Herrmann, C. and Wittinghofer, A. (1999) Structural and biochemical analysis of Ras-effector signaling via RalGDS. FEBS letters 451 (2), pp. 175-180.

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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 beta-sheet between the switch I region of Ras and the second strand of the RGS-RBD sheet, but the details of the interactions ...

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Item Type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
10371160PubMed ID
10.1016/S0014-5793(99)00555-4DOI
Classification:
NotationType
Crystallography, X-RayMESH
GTP-Binding Proteins/physiologyMESH
Gene Products, vpr/physiologyMESH
Models, MolecularMESH
MutagenesisMESH
Protein BindingMESH
Protein ConformationMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
Signal TransductionMESH
ral Guanine Nucleotide Exchange FactorMESH
rap GTP-Binding ProteinsMESH
ras Proteins/physiologyMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:01
Last Modified:13 Sep 2010 08:01
Item ID:16562
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