1qpf: Difference between revisions

Revision as of 20:43, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qpf.png

Template:STRUCTURE 1qpf

FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858

Template:ABSTRACT PUBMED 10425089

About this StructureAbout this Structure

1QPF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 20:43:49 2008

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OCA

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-[[Image:1qpf.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1qpf|  PDB=1qpf  |  SCENE=  }}
-'''FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858'''
+===FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-709,858===
-==Overview==
+<!--
--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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10425089}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10425089 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10425089}}
 ==About this Structure==
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 [[Category: Immunophilin-drug complex]]
 [[Category: Peptidyl-prolyl isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:33:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:43:49 2008''