1rfa
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(New page: 200px<br /> <applet load="1rfa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rfa" /> '''NMR SOLUTION STRUCTURE OF THE RAS-BINDING D...)
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Revision as of 16:56, 12 November 2007
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NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1
Overview
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.
About this Structure
1RFA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface., Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC, Biochemistry. 1995 May 30;34(21):6911-8. PMID:7766599
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