| Budget Amount *help |
¥16,250,000 (Direct Cost: ¥12,500,000、Indirect Cost: ¥3,750,000)
Fiscal Year 2016: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2015: ¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2014: ¥7,150,000 (Direct Cost: ¥5,500,000、Indirect Cost: ¥1,650,000)
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| Outline of Final Research Achievements |
We succeeded in large scale preparation and purification of the post-translationally lipid-modified form of H-Ras protein and various intermediates of the modification by utilizing the protein-ligation reaction catalyzed by Sortase A. Structural analyses of the GTP-bound form of post-translationally-modified H-Ras using nuclear magnetic resonance spectroscopy and X-ray crystallography revealed that the modified C terminus established an intramolecular interaction with the N-terminal catalytic domain of H-Ras and positioned the post-translationally-attached farnesyl moiety at the proximity of the activator region, thereby forming a new binding interface for a Ras effector protein, c-Raf-1.
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