This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1mik
From Proteopedia
Contents |
THE ROLE OF WATER MOLECULES IN THE STRUCTURE-BASED DESIGN OF (5-HYDROXYNORVALINE)-2-CYCLOSPORIN: SYNTHESIS, BIOLOGICAL ACTIVITY, AND CRYSTALLOGRAPHIC ANALYSIS WITH CYCLOPHILIN A
Template:ABSTRACT PUBMED 7650689
About this Structure
1mik is a 2 chain structure of Cyclophilin with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Mikol V, Papageorgiou C, Borer X. The role of water molecules in the structure-based design of (5-hydroxynorvaline)-2-cyclosporin: synthesis, biological activity, and crystallographic analysis with cyclophilin A. J Med Chem. 1995 Aug 18;38(17):3361-7. PMID:7650689
- Mikol V, Duc D. Crystallization of the complex between cyclophilin A and cyclosporin derivatives: the use of cross-seeding. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):543-9. PMID:15299416 doi:10.1107/S0907444994001800
- Mikol V, Kallen J, Pflugl G, Walkinshaw MD. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J Mol Biol. 1993 Dec 20;234(4):1119-30. PMID:8263916 doi:http://dx.doi.org/10.1006/jmbi.1993.1664
