1qpl
From Proteopedia
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| - | [[Image:1qpl.gif|left|200px]] | + | [[Image:1qpl.gif|left|200px]] |
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| - | '''FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587''' | + | {{Structure |
| + | |PDB= 1qpl |SIZE=350|CAPTION= <scene name='initialview01'>1qpl</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=587:C32-O-(1-METHYL-INDOL-5-YL) 18-HYDROXY-ASCOMYCIN'>587</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QPL is a [ | + | 1QPL 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=1QPL OCA]. |
==Reference== | ==Reference== | ||
| - | 32-Indolyl ether derivatives of ascomycin: three-dimensional structures of complexes with FK506-binding protein., Becker JW, Rotonda J, Cryan JG, Martin M, Parsons WH, Sinclair PJ, Wiederrecht G, Wong F, J Med Chem. 1999 Jul 29;42(15):2798-804. PMID:[http:// | + | 32-Indolyl ether derivatives of ascomycin: three-dimensional structures of complexes with FK506-binding protein., Becker JW, Rotonda J, Cryan JG, Martin M, Parsons WH, Sinclair PJ, Wiederrecht G, Wong F, J Med Chem. 1999 Jul 29;42(15):2798-804. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10425089 10425089] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: peptidyl-prolyl isomerase]] | [[Category: peptidyl-prolyl isomerase]] | ||
| - | ''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 13:40:56 2008'' |
Revision as of 11:40, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587
Overview
32-Indole ether derivatives of tacrolimus and ascomycin retain the potent immunosuppressive activity of their parent compounds but display reduced toxicity. In addition, their complexes with the 12-kDa FK506-binding protein (FKBP) form more stable complexes with the protein phosphatase calcineurin, the molecular target of these drugs. We have solved the three-dimensional structures of the FKBP complexes with two 32-indolyl derivatives of ascomycin. The structures of the protein and the macrolide are remarkably similar to those seen in the complexes with tacrolimus and ascomycin. The indole groups project away from the body of the complex, and multiple conformations are observed for the linkage to these groups as well as for a nearby peptide suggesting apparent flexibility in these parts of the structure. Comparison of these structures with that of the ternary complex of calcineurin, FKBP, and tacrolimus suggests that the indole groups interact with a binding site comprising elements of both the calcineurin alpha- and beta-chains and that this interaction is responsible for the increased stability of these complexes.
About this Structure
1QPL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
32-Indolyl ether derivatives of ascomycin: three-dimensional structures of complexes with FK506-binding protein., Becker JW, Rotonda J, Cryan JG, Martin M, Parsons WH, Sinclair PJ, Wiederrecht G, Wong F, J Med Chem. 1999 Jul 29;42(15):2798-804. PMID:10425089
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