2bit
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(New page: 200px<br /> <applet load="2bit" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bit, resolution 1.71Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 18:56, 12 November 2007
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CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION
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Overview
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.
Disease
Known disease associated with this structure: Hypertension, salt-sensitive essential, susceptibility to OMIM:[605325]
About this Structure
2BIT is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Crystal engineering yields crystals of cyclophilin D diffracting to 1.7 A resolution., Schlatter D, Thoma R, Kung E, Stihle M, Muller F, Borroni E, Cesura A, Hennig M, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):513-9. Epub 2005, Apr 20. PMID:15858260
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