Publication Abstract from PubMed
Cyclophilin D (CypD) is a key mitochondrial target for amyloid-beta-induced mitochondrial and synaptic dysfunction and is considered a potential drug target for Alzheimer's disease. The high-resolution crystal structures of primitive orthorhombic (CypD-o) and primitive tetragonal (CypD-t) forms have been determined to 1.45 and 0.85 A resolution, respectively, and are nearly identical structurally. Although an isomorphous structure of CypD-t has previously been reported, the structure reported here was determined at atomic resolution, while CypD-o represents a new crystal form for this protein. In addition, each crystal form contains a PEG 400 molecule bound to the same region along with a second PEG 400 site in CypD-t which occupies the cyclosporine A inhibitor binding site of CypD. Highly precise structural information for CypD should be extremely useful for discerning the detailed interaction of small molecules, particularly drugs and/or inhibitors, bound to CypD. The 0.85 A resolution structure of CypD-t is the highest to date for any CypD structure.
High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.,Valasani KR, Carlson EA, Battaile KP, Bisson A, Wang C, Lovell S, ShiDu Yan S Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):717-22. doi:, 10.1107/S2053230X14009480. Epub 2014 May 24. PMID:24915078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
