Figure 4 - full size

 

Figure 4.
Fig. 4. A: Stereo view of an overlay of the active site of bmCyp-1 (filled bonds) with hCypA (unfilled bonds) showing the side chains of the 13 residues known to be involved in substrate and inhibitor binding of hCypA. The hydrogen bond from the amino nitrogen atom of K114 to the carbonyl O of G83 is shown as a thin line. B: Stereo view of the active site of bmCyp-1 (filled bonds) with the cyclic peptide cyclosporin A (CsA). CsA coordinates are from the hCypA/CsA complex [18] and positioned from the least squares fit used in A. The side chain of K114 in the bmCyp-1 structure acts as a gate to block access to the ‘Abu-pocket' which is a deep accessible cleft in the hCypA structure. C: Stereo view of the active site of bmCyp-1 (filled bonds) showing the position M46 (unfilled bonds) from a crystallographically related neighbouring molecule. M46 forms van der Waals contacts with F71, M72, F124, L133 and H137 and suggests that the hydrophobic active site of cyclophilins may accommodate a range of large hydrophobic groups.

The above figure is reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (1998, 425, 361-366) copyright 1998.