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1x1r
From Proteopedia
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'''Crystal structure of M-Ras in complex with GDP''' | '''Crystal structure of M-Ras in complex with GDP''' | ||
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[[Category: Yamamoto, M.]] | [[Category: Yamamoto, M.]] | ||
[[Category: Ye, M.]] | [[Category: Ye, M.]] | ||
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Revision as of 11:25, 3 May 2008
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.
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 Sat May 3 14:25:12 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
