| Autor: |
S D, Emerson, V S, Madison, R E, Palermo, D S, Waugh, J E, Scheffler, K L, Tsao, S E, Kiefer, S P, Liu, D C, Fry |
| Rok vydání: |
1996 |
| Předmět: |
|
| Zdroj: |
Drug design and discovery. 13(3-4) |
| ISSN: |
1055-9612 |
| Popis: |
The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR spectroscopy is presented. It consists of a five-stranded beta-sheet, a twelve residue alpha-helix, and an additional one-turn helix. The fold belongs to a known family whose members include ubiquitin and protein G. The surface of Raf55-132 that interacts with Ras has been identified by resonance perturbation mapping. The binding site is a spatially contiguous patch comprised of the two-N-terminal beta-strands, the loop between them, and the C-terminal end of the alpha-helix. A model of the Raf-Ras complex is presented, which was derived by analogy to the complex between protein G and a Fab fragment of IgG. In the model, edge beta-strands of each protein align in an antiparallel orientation, forming a unified beta-sheet, and side chains from both proteins are able to participate in ionic and hydrophobic interactions at the interface. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
