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Structural and biochemical analysis of Ras-effector signaling via RalGDS

Vetter, I. R., Linnemann, T., Wohlgemuth, S., Geyer, M., Kalbitzer, Hans Robert, 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
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Item ID:16562
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