2BIU
Crystal structure of human cyclophilin D at 1.7 A resolution, DMSO complex
Summary for 2BIU
| Entry DOI | 10.2210/pdb2biu/pdb |
| Related | 2BIT |
| Descriptor | PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, DIMETHYL SULFOXIDE (3 entities in total) |
| Functional Keywords | crystal engineering, cis-tran-isomerization, human, mitochondrial protein, isomerase |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 18051.74 |
| Authors | Hennig, M.,Thoma, R.,Stihle, M.,Schlatter, D. (deposition date: 2005-01-26, release date: 2005-01-26, Last modification date: 2023-12-13) |
| Primary citation | Schlatter, D.,Thoma, R.,Kueng, E.,Stihle, M.,Mueller, F.,Boroni, E.,Hennig, M. Crystal Engineering Yields Crystals of Cyclophilin D Diffracting to 1.7 A Resolution Acta Crystallogr.,Sect.D, 61:513-519, 2005 Cited by PubMed Abstract: In the pharmaceutical industry, knowledge of the three-dimensional structure of a specific target facilitates the drug-discovery process. Despite possessing favoured analytical properties such as high purity and monodispersion in light scattering, some proteins are not capable of forming crystals suitable for X-ray analysis. Cyclophilin D, an isoform of cyclophilin that is expressed in the mitochondria, was selected as a drug target for the treatment of cardiac disorders. As the wild-type enzyme defied all attempts at crystallization, protein engineering on the enzyme surface was performed. The K133I mutant gave crystals that diffracted to 1.7 A resolution using in-house X-ray facilities and were suitable for soaking experiments. The crystals were very robust and diffraction was maintained after soaking in 25% DMSO solution: excellent conditions for the rapid analysis of complex structures including crystallographic fragment screening. PubMed: 15858260DOI: 10.1107/S0907444905003070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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