2fap
From Proteopedia
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THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA
Overview
The structure of the FKBP12-rapamycin-FRB ternary complex has now been, refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds, FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB), domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and, the inhibition of FRAP is responsible for rapamycin's biological activity., The conformation of rapamycin in the ternary complex is very similar to, that observed in the FKBP12-rapamycin binary complex, with an r.m.s., difference of only 0.30 A. However, a slight (9 degrees ) rotation, repositions the FRB-binding face of rapamycin in the ternary complex., There are extensive rapamycin-protein interactions and relatively few, interactions between the two protein partners FKBP12 and FRB, these, interactions mainly involving residues in the 40s and 80s loops of FKBP12, and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed, the crucial role of several buried waters in the formation of the ternary, complex.
About this Structure
2FAP is a Protein complex structure of sequences from Homo sapiens with RAD as ligand. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution., Liang J, Choi J, Clardy J, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):736-44. PMID:10089303
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