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New page: left|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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[[Image:1rfa.gif|left|200px]]<br />
[[Image:1rfa.gif|left|200px]]<br /><applet load="1rfa" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1rfa" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1rfa" />
caption="1rfa" />
'''NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1'''<br />
'''NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1'''<br />


==Overview==
==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.
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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164760 164760]], Noonan syndrome 5 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164760 164760]]


==About this Structure==
==About this Structure==
1RFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RFA OCA].  
1RFA is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Emerson, S.D.]]
[[Category: Emerson, S D.]]
[[Category: Fry, D.C.]]
[[Category: Fry, D C.]]
[[Category: Kiefer, S.E.]]
[[Category: Kiefer, S E.]]
[[Category: Liu, S.P.]]
[[Category: Liu, S P.]]
[[Category: Madison, V.S.]]
[[Category: Madison, V S.]]
[[Category: Palermo, R.E.]]
[[Category: Palermo, R E.]]
[[Category: Scheffler, J.E.]]
[[Category: Scheffler, J E.]]
[[Category: Tsao, K.L.]]
[[Category: Tsao, K L.]]
[[Category: Waugh, D.S.]]
[[Category: Waugh, D S.]]
[[Category: serine/threonine-protein kinase]]
[[Category: serine/threonine-protein kinase]]
[[Category: signal transduction protein]]
[[Category: signal transduction protein]]


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