Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52.

Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form I

Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Ii

Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iii

Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iv

Fk1 Domain Mutant A19t Of Fkbp51, Crystal Form Iv, In Presence Of Dmso

Complex Of Fk506 With The Fk1 Domain Mutant A19t Of Fkbp51

Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor At Low Ph

Co-crystal Structure Of The Ppiase Domain Of Fkbp51, Rapamycin And The Frb Fragment Of Mtor

Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With {3-[(1r)-3-(3,4-Dimethoxyphenyl)

Evaluation Of Synthetic Fk506 Analogs As Ligands For Fkbp51 And Fkbp52: Complex Of Fkbp51 With (1r)-3-(3,4-Dimethoxyphenyl)-1-

Evaluation Of Synthetic Fk506 Analogs As Ligands For The Fk506-Binding Proteins 51 And 52: Complex Of Fkbp51 With 2-(3-((R)-3-(

Exploration Of Pipecolate Sulfonamides As Binders Of The Fk506-Binding Proteins 51 And 52: Complex Of Fkbp51 With 2-(3-((R)-1-(

Increasing The Efficiency Efficiency Of Ligands For The Fk506-binding Protein 51 By Conformational Control: Complex Of Fkbp51 W

Allosteric Coupling Of Conformational Transitions In The Fk1 Domain Of Fkbp51 Near The Site Of Steroid Receptor Interaction

The Fk1 Domain Of Fkbp51 In Complex With Ifit1

The Fk1 Domain Of Fkbp51 In Complex With Ifit4

The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3

The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-[(1r)-1,2-dihydroxyethyl]-3-[2-(3,4- D

The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-5-[(1s)-1,2-dihydroxyethyl]-3-[2-(3,4- D

The Fk1 Domain Of Fkbp51 In Complex With (1s,5s,6r)-10-[(3,5- Dichlorophenyl)sulfonyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-5-ethy

The Fk1 Domain Of Fkbp51 In Complex With The New Synthetic Ligand (1r)-3-(3,4-dimethoxyphenyl)-1-f3-[2-(morpholin-4-yl) Ethoxy]

FK506 binding protein 5 variant [Homo sapiens]

peptidyl-prolyl cis-trans isomerase FKBP5 isoform 2 [Homo sapiens]

PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5-like [Papio anubis]

PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X2 [Orcinus orca]

PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X6 [Sus scrofa]

PREDICTED: peptidyl-prolyl cis-trans isomerase FKBP5 isoform X7 [Sus scrofa]

School of Public Health, University at Albany SUNY

X-ray structure of FKBP51-FK506 binding domain 1