Conformational differences of an immunosuppressant peptolide in a single crystal and in a crystal complex with human cyclophilin A

V Mikol, P Taylor, J Kallen, M D Walkinshaw

Research output: Contribution to journalArticlepeer-review

Abstract

The crystal structure of (Thr2, Leu5, d-Hiv8, Leu10)-cyclosporin (cyclic peptolide SDZ 214-103) has been determined as the unbound crystal form and as a complex with human cyclophilin A. This pair of structures provides an example of a significant difference in conformation between free and bound ligand in crystals. The conformation of the unbound form is unlike that of both free and bound conformations of cyclosporin A (with the amide bond between residues 3 and 4 in the cis conformation), while the bound conformation is similar to that of CsA bound to cyclophilin. The cyclophilin-bound conformations of both ligands are similar, though this involves a significantly different waterellipsisligand hydrogen-bonding structure, which compensates for the chemical differences between the two ligands.
Original languageEnglish
Pages (from-to)451-61
Number of pages11
JournalJournal of Molecular Biology
Volume283
Issue number2
DOIs
Publication statusPublished - 1998

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