1EF5
SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL
Summary for 1EF5
| Entry DOI | 10.2210/pdb1ef5/pdb |
| Descriptor | RGL (1 entity in total) |
| Functional Keywords | ras-binding domain, rgl, ras, rbd, ra, riken structural genomics/proteomics initiative, rsgi, structural genomics, signaling protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 11737.15 |
| Authors | Kigawa, T.,Endo, M.,Ito, Y.,Shirouzu, M.,Kikuchi, A.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2000-02-07, release date: 2000-02-23, Last modification date: 2024-05-22) |
| Primary citation | Kigawa, T.,Endo, M.,Ito, Y.,Shirouzu, M.,Kikuchi, A.,Yokoyama, S. Solution structure of the Ras-binding domain of RGL. FEBS Lett., 441:413-418, 1998 Cited by PubMed Abstract: The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD. PubMed: 9891982DOI: 10.1016/S0014-5793(98)01596-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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