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- Title
Thermodynamic characterization of OsGID1-gibberellin binding using calorimetry and docking simulations.
- Authors
Xiang, Hongyu; Takeuchi, Hiromi; Tsunoda, Yuki; Nakajima, Masatoshi; Murata, Katsuyoshi; Ueguchi-Tanaka, Miyako; Kidokoro, Shun-ichi; Kezuka, Yuichiro; Nonaka, Takamasa; Matsuoka, Makoto; Katoh, Etsuko
- Abstract
The article determines the types of forces important to binding via a combination of isothermal titration calorimetry (ITC) and computational docking studies that employed gibberellin (GA) variants, rice GA receptor protein GID1 (OsGID1), and OsGID1 mutants. The results suggested that GA binding is generally enthalpically driven. The significance of a hydrogen bond between the phenolic hydroxyl of OsGID1 Tyr134 and the C-3 hydroxyl of a GA as a defining structural element is also discussed.
- Subjects
CALORIMETRY; GIBBERELLINS; PROTEINS; MOLECULAR recognition; MOLECULAR biology
- Publication
Journal of Molecular Recognition, 2011, Vol 24, Issue 2, p275
- ISSN
0952-3499
- Publication type
Article
- DOI
10.1002/jmr.1049