1LFD
CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS
Summary for 1LFD
| Entry DOI | 10.2210/pdb1lfd/pdb |
| Descriptor | RALGDS, RAS, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | complex (ralgds-ras), ral, effector interaction, complex (ralgds-ras) complex, complex (ralgds/ras) |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cytoplasm : Q03386 Cell membrane. Isoform 2: Nucleus: P01112 |
| Total number of polymer chains | 4 |
| Total formula weight | 59080.50 |
| Authors | Huang, L.,Hofer, F.,Martin, G.S.,Kim, S.-H. (deposition date: 1998-04-29, release date: 1999-05-04, Last modification date: 2024-05-22) |
| Primary citation | Huang, L.,Hofer, F.,Martin, G.S.,Kim, S.H. Structural basis for the interaction of Ras with RalGDS. Nat.Struct.Biol., 5:422-426, 1998 Cited by PubMed Abstract: The Ras protein signals to a number of distinct pathways by interacting with diverse downstream effectors. Among the effectors of Ras are the Raf kinase and RalGDS, a guanine nucleotide dissociation stimulator specific for Ral. Despite the absence of significant sequence similarities, both effectors bind directly to Ras, but with different specificities. We report here the 2.1 A crystal structure of the complex between Ras and the Ras-interacting domain (RID) of RalGDS. This structure reveals that the beta-sheet of the RID joins the switch I region of Ras to form an extended beta-sheet with a topology similar to that found in the Rap-Raf complex. However, the side chain interactions at the joining junctions of the two interacting systems and the relative orientation of the two binding domains are distinctly different. Furthermore, in the case of the Ras-RID complex a second RID molecule also interacts with a different part of the Ras molecule, the switch II region. These findings account for the cross-talk between the Ras and Ral pathways and the specificity with which Ras distinguishes the two effectors. PubMed: 9628477DOI: 10.1038/nsb0698-422 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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