From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1x1r.gif|left|200px]] | + | {{Seed}} |
| + | [[Image:1x1r.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1x1r| PDB=1x1r | SCENE= }} | | {{STRUCTURE_1x1r| PDB=1x1r | SCENE= }} |
| | | |
- | '''Crystal structure of M-Ras in complex with GDP'''
| + | ===Crystal structure of M-Ras in complex with GDP=== |
| | | |
| | | |
- | ==Overview==
| + | <!-- |
- | Although some members of Ras family small GTPases, including M-Ras, share the primary structure of their effector regions with Ras, they exhibit vastly different binding properties to Ras effectors such as c-Raf-1. We have solved the crystal structure of M-Ras in the GDP-bound and guanosine 5'-(beta,gamma-imido)triphosphate (Gpp(NH)p)-bound forms. The overall structure of M-Ras resembles those of H-Ras and Rap2A, except that M-Ras-Gpp(NH)p exhibits a distinctive switch I conformation, which is caused by impaired intramolecular interactions between Thr-45 (corresponding to Thr-35 of H-Ras) of the effector region and the gamma-phosphate of Gpp(NH)p. Previous 31P NMR studies showed that H-Ras-Gpp(NH)p exists in two interconverting conformations, states 1 and 2. Whereas state 2 is a predominant form of H-Ras and corresponds to the "on" conformation found in the complex with effectors, state 1 is thought to represent the "off" conformation, whose tertiary structure remains unknown. 31P NMR analysis shows that free M-Ras-Gpp(NH)p predominantly assumes the state 1 conformation, which undergoes conformational transition to state 2 upon association with c-Raf-1. These results indicate that the solved structure of M-Ras-Gp-p(NH)p corresponds to the state 1 conformation. The predominance of state 1 in M-Ras is likely to account for its weak binding ability to the Ras effectors, suggesting the importance of the tertiary structure factor in small GTPase-effector interaction. Further, the first determination of the state 1 structure provides a molecular basis for developing novel anti-cancer drugs as compounds that hold Ras in the state 1 "off" conformation.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15994326}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 15994326 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_15994326}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 33: |
Line 37: |
| [[Category: Ye, M.]] | | [[Category: Ye, M.]] |
| [[Category: Gtp-binding]] | | [[Category: Gtp-binding]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:25:12 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:51:19 2008'' |
Revision as of 03:51, 29 July 2008
Template:STRUCTURE 1x1r
Crystal structure of M-Ras in complex with GDP
Template:ABSTRACT PUBMED 15994326
About this Structure
1X1R is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of M-Ras reveals a GTP-bound "off" state conformation of Ras family small GTPases., Ye M, Shima F, Muraoka S, Liao J, Okamoto H, Yamamoto M, Tamura A, Yagi N, Ueki T, Kataoka T, J Biol Chem. 2005 Sep 2;280(35):31267-75. Epub 2005 Jun 30. PMID:15994326
Page seeded by OCA on Tue Jul 29 06:51:19 2008
Categories: Mus musculus | Single protein | Kataoka, T. | Liao, J. | Muraoka, S. | Okamoto, H. | Shima, F. | Tamura, A. | Ueki, T. | Yagi, N. | Yamamoto, M. | Ye, M. | Gtp-binding