1yat
From Proteopedia
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| - | [[Image:1yat.jpg|left|200px]] | + | [[Image:1yat.jpg|left|200px]] |
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| - | '''IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS''' | + | {{Structure |
| + | |PDB= 1yat |SIZE=350|CAPTION= <scene name='initialview01'>1yat</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YAT is a [ | + | 1YAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YAT OCA]. |
==Reference== | ==Reference== | ||
| - | Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis., Rotonda J, Burbaum JJ, Chan HK, Marcy AI, Becker JW, J Biol Chem. 1993 Apr 15;268(11):7607-9. PMID:[http:// | + | Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis., Rotonda J, Burbaum JJ, Chan HK, Marcy AI, Becker JW, J Biol Chem. 1993 Apr 15;268(11):7607-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7681823 7681823] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: binding protein]] | [[Category: binding 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 15:20:36 2008'' |
Revision as of 13:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS
Overview
The protein phosphatase calcineurin is the putative target for the immunosuppressive drug FK-506. The enzyme is inhibited by the complex of the drug with its intracellular receptor, the 12-kDa FK-506-binding protein (FKBP12), and the strength of inhibition usually correlates strongly with immunosuppressive potency. We find, however, that the complex of yeast FKBP12 with L-685,818, a well characterized antagonist of FK-506 immunosuppression, is a potent inhibitor of calcineurin. The corresponding human complex does not inhibit the enzyme, and both human and yeast complexes with FK-506 do inhibit. To understand the structural basis of these findings, we have determined the three-dimensional structure of the complex of yeast FKBP12 with FK-506 by x-ray crystallography, and have found that the structure of the yeast complex is strikingly similar to its human homolog. These observations indicate that specific sequence elements in the yeast protein provide stronger binding interactions with a heterologous calcineurin than do the corresponding elements in the human protein, and suggest structural modifications that may improve the potency of this class of immunosuppressants.
About this Structure
1YAT is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis., Rotonda J, Burbaum JJ, Chan HK, Marcy AI, Becker JW, J Biol Chem. 1993 Apr 15;268(11):7607-9. PMID:7681823
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