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Molecular‐mechanical studies of hormone–protein interactions: The interaction of T 4 and T 3 with prealbumin
Author(s) -
Oatley Stuart J.,
Blaney Jeffrey M.,
Langridge Robert,
Kollman Peter A.
Publication year - 1984
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360231215
Subject(s) - chemistry , solvation , transthyretin , thyronine , binding energy , molecular dynamics , hormone , computational chemistry , thermodynamics , molecule , crystallography , thyroid hormones , atomic physics , physics , organic chemistry , biochemistry , medicine
We present molecular‐mechanical calculations on the interactions of L ‐thyroxine (T 4 ) and 3,5,3′‐triiodo‐ L ‐thyronine (T 3 ) with the binding site of human serum prealbumin. Energy refinement with restraints on the movement of the iodine atoms leads to reasonably low‐energy structures with the iodines within 0.2 Å of their x‐ray determined positions; removal of these restraints leads to larger (∼1.0 Å) deviations from these positions. However the relative energies of T 3 and T 4 complexation are similar in both cases, and the relative calculated energies for these complexes, when corrected by a simple empirical method for the solvation energy differences of the hormones, are in reasonable qualitative agreement with experiment.