Structural basis for intramolecular interaction of post‐translationally modified H‐Ras•GTP prepared by protein ligation
2017
Ke, Haoliang | Matsumoto, Shigeyuki | Murashima, Yosuke | Taniguchi‐Tamura, Haruka | Miyamoto, Ryo | Yoshikawa, Yōko | Tsuda, Chiemi | Kumasaka, Takashi | Mizohata, Eiichi | Edamatsu, Hironori | Kataoka, Tohru
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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