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'''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION''' | '''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION''' | ||
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[[Category: Stihle, M.]] | [[Category: Stihle, M.]] | ||
[[Category: Thoma, R.]] | [[Category: Thoma, R.]] | ||
[[Category: | [[Category: Cis-tran-isomerization]] | ||
[[Category: | [[Category: Crystal engineering]] | ||
[[Category: | [[Category: Human]] | ||
[[Category: | [[Category: Isomerase]] | ||
[[Category: | [[Category: Mitochondrial protein]] | ||
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Revision as of 17:21, 3 May 2008
CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION
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.
About this Structure
2BIT is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sat May 3 20:21:00 2008
