Fragment molecular orbital study of the binding energy of ligands to the estrogen receptor

Kaori Fukuzawa, Kazuo Kitaura, Kotoko Nakata, Tsuguchika Kaminuma, Tatsuya Nakano

研究成果: ジャーナルへの寄稿学術論文査読

23 被引用数 (Scopus)

抄録

We examined the published data for the binding affinity of typical ligands to the α-subtype of the human estrogen receptor with use of an approximate molecular orbital method applicable to interacting molecular clusters. An ab initio procedure for "molecular fragments" proposed recently to deal with such macromolecules as proteins was applied to the molecular orbital calculations. The receptor protein was primarily modeled using 50 amino acid residues surrounding the ligand. For a few ligand-receptor complexes, the binding energy was also calculated with use of 241 amino acid residues contained in the entire binding domain. No significant difference was found in the calculated binding energy between the complex modeled with ligand-surrounding 50 amino acids and that with residues of the entire domain. The calculated binding energy was correlated very well with the published relative binding affinity for typical ligands.

本文言語英語
ページ(範囲)2405-2410
ページ数6
ジャーナルPure and Applied Chemistry
75
11-12
DOI
出版ステータス出版済み - 2003

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