Title : Mean field analysis of FKBP12 complexes with FK506 and rapamycin: implications for a role of crystallographic water molecules in molecular recognition and specificity.

Pub. Date : 1997 Jul

PMID : 9223178






7 Functional Relationships(s)
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1 Mean field analysis of FKBP12 complexes with FK506 and rapamycin: implications for a role of crystallographic water molecules in molecular recognition and specificity. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
2 Mean field analysis of FKBP12 complexes with FK506 and rapamycin has been performed by using structures obtained from molecular docking simulations on a simple, yet robust molecular recognition energy landscape. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
3 The stability gap in the FKBP12-FK506 system is determined by two critical water molecules from the effector region that participate in a network of specific hydrogen bond interactions. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
4 This interaction pattern protects the integrity and precision of the composite ligand-protein effector surface in the binary FKBP12-FK506 complex and is preserved in the crystal structure of the FKBP12-FK506-calcineurin ternary complex. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
5 This interaction pattern protects the integrity and precision of the composite ligand-protein effector surface in the binary FKBP12-FK506 complex and is preserved in the crystal structure of the FKBP12-FK506-calcineurin ternary complex. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
6 This interaction pattern protects the integrity and precision of the composite ligand-protein effector surface in the binary FKBP12-FK506 complex and is preserved in the crystal structure of the FKBP12-FK506-calcineurin ternary complex. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens
7 This interaction pattern protects the integrity and precision of the composite ligand-protein effector surface in the binary FKBP12-FK506 complex and is preserved in the crystal structure of the FKBP12-FK506-calcineurin ternary complex. Tacrolimus FKBP prolyl isomerase 1A pseudogene 4 Homo sapiens