1RFA

NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1

Summary for 1RFA

• Entry DOI: 10.2210/pdb1rfa/pdb
• Descriptor: RAF1 (1 entity in total)
• Functional Keywords: serine/threonine-protein kinase, signal transduction protein, serine-threonine-protein kinase complex
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): P04049
• Total number of polymer chains: 1
• Total formula weight: 8975.45

Authors

Emerson, S.D.,Madison, V.S.,Palermo, R.E.,Waugh, D.S.,Scheffler, J.E.,Tsao, K.-L.,Kiefer, S.E.,Liu, S.P.,Fry, D.C. (deposition date: 1995-04-26, release date: 1996-06-20, Last modification date: 2024-05-22)

Primary citation

Emerson, S.D.,Madison, V.S.,Palermo, R.E.,Waugh, D.S.,Scheffler, J.E.,Tsao, K.L.,Kiefer, S.E.,Liu, S.P.,Fry, D.C.
Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface.
Biochemistry, 34:6911-6918, 1995

PubMed Abstract: The structure of the Ras-binding domain of human c-Raf-1 (residues 55-132) has been determined in solution by nuclear magnetic resonance (NMR) spectroscopy. Following complete assignment of the backbone and side-chain 1H, 15N, and 13C resonances, the structure was calculated using the program CHARMM. Over 1300 NOE-derived constraints were applied, resulting in a detailed structure. The fold of Raf55-132 consists of a five-stranded beta-sheet, a 12-residue alpha-helix, and an additional one-turn helix. It is similar to those of ubiquitin and the IgG-binding domain of protein G, although the three proteins share very little sequence identity. The surface of Raf55-132 that interacts with Ras has been identified by monitoring perturbation of line widths and chemical shifts of 15N-labeled Raf55-132 resonances during titration with unlabeled Ras-GMPPNP. The Ras-binding site is contained within a spatially contiguous patch comprised of the N-terminal beta-hairpin and the C-terminal end of the alpha-helix.

PubMed: 7766599
DOI: 10.1021/bi00021a001

Experimental method

SOLUTION NMR