学術雑誌論文 Structural basis for intramolecular interaction of post-translationally modified H-Ras.GTP prepared by protein ligation

Ke, Haoliang  ,  Matsumoto, Shigeyuki  ,  Murashima, Yosuke  ,  Taniguchi-Tamura, Haruka  ,  Miyamoto, Ryo  ,  Yoshikawa, Yoko  ,  Tsuda, Chiemi  ,  Kumasaka, Takashi  ,  Mizohata, Eiichi  ,  Edamatsu, Hironori  ,  Kataoka, Tohru

591 ( 16 )  , pp.2470 - 2481 , 2017-08 , John Wiley and Sons
ISSN:0014579318733468
内容記述
Ras undergoes post-translational modifications including farnesylation, proteolysis, and carboxymethylation at the C terminus, which are necessary for membrane recruitment and effector recognition. Full activation of c-Raf-1 requires cooperative interaction of the farnesylated C terminus and the activator region of Ras with its cysteine-rich domain (CRD). However, the molecular basis for this interaction remains unclear because of difficulties in preparing modified Ras in amounts sufficient for structural studies. Here, we use Sortase A-catalyzed protein ligation to prepare modified Ras in sufficient amounts for NMR and X-ray crystallographic analyses. The results show that the farnesylated C terminus establishes an intramolecular interaction with the catalytic domain and brings the farnesyl moiety to the proximity of the activator region, which may be responsible for their cooperative recognition of c-Raf-1-CRD.
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http://www.lib.kobe-u.ac.jp/repository/90004244.pdf

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