3fap

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spinqualitylabelsall models 3fap, resolution 1.850Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP

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

3FAP is a Protein complex structure of sequences from Homo sapiens with ARD 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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