1rfa
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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=" | + | |
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) | + | 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:// | + | 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== | ||
| Line 14: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Emerson, S | + | [[Category: Emerson, S D.]] |
| - | [[Category: Fry, D | + | [[Category: Fry, D C.]] |
| - | [[Category: Kiefer, S | + | [[Category: Kiefer, S E.]] |
| - | [[Category: Liu, S | + | [[Category: Liu, S P.]] |
| - | [[Category: Madison, V | + | [[Category: Madison, V S.]] |
| - | [[Category: Palermo, R | + | [[Category: Palermo, R E.]] |
| - | [[Category: Scheffler, J | + | [[Category: Scheffler, J E.]] |
| - | [[Category: Tsao, K | + | [[Category: Tsao, K L.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: serine/threonine-protein kinase]] | [[Category: serine/threonine-protein kinase]] | ||
[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:15 2008'' |
Revision as of 12:50, 21 February 2008
|
NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1
Contents |
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
Page seeded by OCA on Thu Feb 21 14:50:15 2008
