2bit: Difference between revisions
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[[Image:2bit.gif|left|200px]] | [[Image:2bit.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION''' | {{Structure | ||
|PDB= 2bit |SIZE=350|CAPTION= <scene name='initialview01'>2bit</scene>, resolution 1.71Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BIT is a [ | 2BIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15858260 15858260] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: mitochondrial protein]] | [[Category: mitochondrial protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:29 2008'' | ||
Revision as of 14:02, 20 March 2008
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| 2bit, resolution 1.71Å | |||||||||||||
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| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
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. 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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