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Article

Oncogenic mutations Q61L and Q61H confer active form-like structural features to the inactive state (state 1) conformation of H-Ras protein.

Biochemical and biophysical research communications - 6 Aug 2021

Matsumoto Shigeyuki, Taniguchi-Tamura Haruka, Araki Mitsugu, Kawamura Takashi, Miyamoto Ryo, Tsuda Chiemi, Shima Fumi, Kumasaka Takashi, Okuno Yasushi, Kataoka Tohru

Abstract excerpt

GTP-bound forms of Ras proteins (Ras•GTP) assume two interconverting conformations, "inactive" state 1 and "active" state 2. Our previous study on the crystal structure of the state 1 conformation of H-Ras in complex with guanosine 5'-(β, γ-imido)triphosphate (GppNHp) indicated that state 1 is stabilized by intramolecular hydrogen-bonding interactions formed by Gln61. Since Ras are constitutively activated by...

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PMID: 34102474
DOI: 10.1016/j.bbrc.2021.05.084

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