1x1r

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[[Image:1x1r.gif|left|200px]]
[[Image:1x1r.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1x1r", creates the "Structure Box" on the page.
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|RELATEDENTRY=[[1x1s|1X1S]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1r OCA], [http://www.ebi.ac.uk/pdbsum/1x1r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x1r RCSB]</span>
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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.]]
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[[Category: gtp-binding]]
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[[Category: Gtp-binding]]
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Revision as of 11:25, 3 May 2008

Image:1x1r.gif

Template:STRUCTURE 1x1r

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

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