4O8H
0.85A resolution structure of PEG 400 Bound Cyclophilin D
Summary for 4O8H
| Entry DOI | 10.2210/pdb4o8h/pdb |
| Related | 4O8I |
| Descriptor | Peptidyl-prolyl cis-trans isomerase F, mitochondrial, DI(HYDROXYETHYL)ETHER, PENTAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | isomerase |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion matrix : P30405 |
| Total number of polymer chains | 1 |
| Total formula weight | 18083.60 |
| Authors | Lovell, S.,Valasani, K.R.,Battaile, K.P.,Wang, C.,Yan, S.S. (deposition date: 2013-12-27, release date: 2014-06-11, Last modification date: 2023-09-20) |
| Primary citation | Valasani, K.R.,Carlson, E.A.,Battaile, K.P.,Bisson, A.,Wang, C.,Lovell, S.,ShiDu Yan, S. High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules. Acta Crystallogr F Struct Biol Commun, 70:717-722, 2014 Cited by PubMed Abstract: 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. PubMed: 24915078DOI: 10.1107/S2053230X14009480 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.85 Å) |
Structure validation
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