Figure 3 - full size


Figure 3.
Figure 3 (a) Overlay of native hCypA (cyan) with hCypA-ACMPIP (atom-type colours). Close contacts between the ACMPIP ligand with surrounding atoms are shown. ACMPIP makes one hydrogen bond to Asn102 N (2.8 ). The most hydrophobic part of the ACMPIP molecule (the methylpiperidine ring) fits into the hydrophobic pocket. van der Waals contacts are made from the ligand to the side chains of six amino acids (Arg55, Phe 60, Met61, Gln63, Phe113 and His126). (b) Overlay of native hCypA (cyan) with the hCypA-ETPIPG in both binding modes (ALT2, green; ALT1, purple). The main difference between the native protein structure and the structure with ETPIPG in the binding site is the movement of the side chain of Met61. The overall backbone conformations of the three structures are very similar. An r.m.s. fit of all protein atoms except residues 1-4, 67-76 and 162-165 between native and the ACMPIP complex is 0.286 and that between the ACMPIP and ETPIPG complexes is 0.367 .

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 479-485) copyright 2004.