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Molecular docking study of binding of TMPyP4 to a bimolecular human telomeric G-quadruplex
Yoshinobu Ishikawa1, Satoshi Fujii
1School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka-shi, Shizuoka 422-8526, Japan. ishi206@u-shizuoka-ken.ac.jp
Nucleic Acids Symposium Series (2004)
|September 9, 2008
Abstract:
We carried out molecular docking simulation of binding of cationic porphyrin TMPyP4 to a bimolecular human telomeric G-quadruplex using DOCK6.1 to examine whether or not to reproduce the loop binding mode of TMPyP4 in the crystal structure. The simulation gave the two highest-ranked docking poses of TMPyP4, and the binding modes were external stacking on the terminal guanine-tetrad and groove binding.

