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High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules

High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules

Acta Crystallographica. Section F Structural Biology Communications 70(Part 6): 717-722

ISSN/ISBN: 2053-230X

PMID: 24915078

DOI: 10.1107/s2053230x14009480

Cyclophilin D (CypD) is a key mitochondrial target for amyloid-β-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 Å 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 Å resolution structure of CypD-t is the highest to date for any CypD structure.

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Accession: 053549407

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