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

Autor:	V, Mikol, P, Taylor, J, Kallen, M D, Walkinshaw
Rok vydání:	1998
Předmět:	Models Molecular X-Ray Diffraction Macromolecular Substances Protein Conformation Humans Cyclosporins Immunophilins Peptidylprolyl Isomerase Immunosuppressive Agents
Zdroj:	Journal of molecular biology. 283(2)
ISSN:	0022-2836
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::c9d569c95f7bd5e6a58564cbab2f1bac https://pubmed.ncbi.nlm.nih.gov/9769217 Zobrazit plný text záznamu Full Text from ScienceDirect