2RMC

Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A

Summary for 2RMC

• Entry DOI: 10.2210/pdb2rmc/pdb
• Related: 1BCK 1C5F 1CSA 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1CYA 1CYB 1CYN 1IKF 1M63 1MF8 1MIK 1QNG 1QNH 1XQ7 2ESL 2OJU 2POY 2RMA 2RMB 2WFJ 2X2C 2X7K 2Z6W 3BO7 3CYS 3EOV
• Related PRD ID: PRD_000142
• Descriptor: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C, CYCLOSPORIN A (3 entities in total)
• Functional Keywords: isomerase-immunosuppressant complex, cyclophilin-cyclosporin complex, cyclosporin a, immunosuppressant, cyclophilin, isomerase/immunosuppressant
• Biological source: MUS MUSCULUS; More
• Cellular location: Cytoplasm: P30412
• Total number of polymer chains: 8
• Total formula weight: 84649.23

Authors

Ke, H.,Zhao, Y.,Luo, F.,Weissman, I.,Friedman, J. (deposition date: 1994-01-07, release date: 1995-02-14, Last modification date: 2023-12-06)

Primary citation

Ke, H.,Zhao, Y.,Luo, F.,Weissman, I.,Friedman, J.
Crystal Structure of Murine Cyclophilin C Complexed with Immunosuppressive Drug Cyclosporin A
Proc.Natl.Acad.Sci.USA, 90:11850-, 1993

PubMed Abstract: Cyclophilin is a cellular receptor for the immunosuppressive drug cyclosporin A (CsA). Cyclophilin C (CyPC) is highly expressed in murine kidney, making it a potential mediator of the nephrotoxic effects of CsA. The structure of murine CyPC complexed with CsA has been solved and refined to an R factor of 0.197 at a 1.64-A resolution. Superposition of the CyPC-CsA structure with the unligated cyclophilin A (CyPA) revealed significant migration of three loops: Gln-179 to Thr-189, Asp-47 to Lys-49, and Met-170 to Ile-176. The proximity of the loop Gln-179 to Thr-189 to the CsA binding site may account for the unique binding of a 77-kDa glycoprotein, CyPC binding protein (CyCAP), to CyPC. The binding of CsA to CyPC is similar to that of CsA to human T-cell cyclophilin A (CyPA). However, the conformation of CsA when bound to CyPC is significantly different from that when bound to CyPA. These differences may reflect conformational variation of CsA when bound to different proteins. Alternatively, the previous CyPA-CsA structure at low resolution may not provide sufficient details for a comparison with the CyPC-CsA structure.

PubMed: 8265636
DOI: 10.1073/PNAS.90.24.11850

Experimental method

X-RAY DIFFRACTION (1.64 Å)