1rfa: Difference between revisions
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[[Image:1rfa.gif|left|200px]] | [[Image:1rfa.gif|left|200px]] | ||
'''NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1''' | {{Structure | ||
|PDB= 1rfa |SIZE=350|CAPTION= <scene name='initialview01'>1rfa</scene> | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RFA is a [ | 1RFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7766599 7766599] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:50:48 2008'' | ||
Revision as of 11:50, 20 March 2008
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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.
Disease
Known diseases associated with this structure: LEOPARD syndrome 2 OMIM:[164760], Noonan syndrome 5 OMIM:[164760]
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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