Three-dimensional structure of the Ras-interacting domain of RalGDS
Open Access
- 1 August 1997
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (8) , 609-615
- https://doi.org/10.1038/nsb0897-609
Abstract
The Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.Keywords
This publication has 43 references indexed in Scilit:
- Ras/Rap effector specificity determined by charge reversalNature Structural & Molecular Biology, 1996
- Differential Interaction of the Ras Family GTP-binding Proteins H-Ras, Rap1A, and R-Ras with the Putative Effector Molecules Raf Kinase and Ral-Guanine Nucleotide Exchange FactorPublished by Elsevier ,1996
- The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogueNature, 1995
- Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] (iron-sulfur) ferredoxin from Anabaena 7120 determined to 1.7-.ANG. resolutionBiochemistry, 1993
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron RadiationScience, 1991
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- ras GENESAnnual Review of Biochemistry, 1987
- Structure of ubiquitin refined at 1.8 Å resolutionJournal of Molecular Biology, 1987
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983