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PDBsum entry 4o8i
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References listed in PDB file
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Key reference
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Title
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High-Resolution crystal structures of two crystal forms of human cyclophilin d in complex with peg 400 molecules.
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Authors
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K.R.Valasani,
E.A.Carlson,
K.P.Battaile,
A.Bisson,
C.Wang,
S.Lovell,
S.Shidu yan.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2014,
70,
717-722.
[DOI no: ]
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PubMed id
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Abstract
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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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