2bit

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[[Image:2bit.gif|left|200px]]<br /><applet load="2bit" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bit.gif|left|200px]]
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caption="2bit, resolution 1.71&Aring;" />
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'''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION'''<br />
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{{Structure
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|PDB= 2bit |SIZE=350|CAPTION= <scene name='initialview01'>2bit</scene>, resolution 1.71&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D AT 1.7 A RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIT OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15858260 15858260]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:19 2008''
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''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


PDB ID 2bit

Drag the structure with the mouse to rotate
, resolution 1.71Å
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


Contents

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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