TY - JOUR
T1 - Fragment molecular orbital study of the binding energy of ligands to the estrogen receptor
AU - Fukuzawa, Kaori
AU - Kitaura, Kazuo
AU - Nakata, Kotoko
AU - Kaminuma, Tsuguchika
AU - Nakano, Tatsuya
PY - 2003/1/1
Y1 - 2003/1/1
N2 - 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.
AB - 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.
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U2 - 10.1351/pac200375112405
DO - 10.1351/pac200375112405
M3 - Article
AN - SCOPUS:1642434179
VL - 75
SP - 2405
EP - 2410
JO - Pure and Applied Chemistry
JF - Pure and Applied Chemistry
SN - 0033-4545
IS - 11-12
ER -