SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROPHIC LIGAND
Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics.
Neurotrophic Immunophilin Ligands Stimulate Structural and Functional Recovery in Neurodegenerative Animal Models
Atomic Structure of FKBP-FK506, an Immunophilin-immunosuppressant Complex
Design, Synthesis, and Kinetic Evaluation of high-affinity FKBP Ligands and the X-ray Structure of their Complexes with FKBP12
15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcinerin Inhibition
PROTEIN COORDINATES WERE TAKEN FROM THE CRYSTAL STRUCTURE BY HOLT ET AL. (1993, PDB ACCESSION CODE 1FKG).
GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFDVELLKLE
1fkg contains the same protein complexed with FK506
1fkg contains the same protein complexed with a non-macrocyclic FK506 analogue
structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations
Structures were calculated using a total of 50 ligand-ligand and 18 protein-ligand distance restraints. NOEs involving degenerate protons were incorporated as ambiguous restraints.
0.5 mM FKBP12 U-15N; 100 mM phosphate buffer; 0.01% NaN3
0.5 mM FKBP12 U-15N; 1mM GPI-1046; 100 mM phosphate buffer; 0.01% NaN3
2mM FKBP12 U-15N,13C; 2mM GPI-1046; 100 mM phosphate buffer; 0.01% NaN3