1fkk: Difference between revisions

Revision as of 03:24, 1 July 2008

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File:1fkk.png

Template:STRUCTURE 1fkk

ATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEINATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEIN

Template:ABSTRACT PUBMED 15299838

About this StructureAbout this Structure

1FKK is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin., Wilson KP, Yamashita MM, Sintchak MD, Rotstein SH, Murcko MA, Boger J, Thomson JA, Fitzgibbon MJ, Black JR, Navia MA, Acta Crystallogr D Biol Crystallogr. 1995 Jul 1;51(Pt 4):511-21. PMID:15299838

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OCA

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-'''ATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEIN'''
+===ATOMIC STRUCTURE OF FKBP12, AN IMMUNOPHILIN BINDING PROTEIN===
-==Overview==
+<!--
-FK506 (tacrolimus) is a natural product now approved in the US and Japan for organ transplantation. FK506, in complex with its 12 kDa cytosolic receptor (FKBP12), is a potent agonist of immunosuppression through the inhibition of the phosphatase activity of calcineurin. Rapamycin (sirolimus), which is itself an immunosuppressant by a different mechanism, completes with FK506 for binding to FKBP12 and thereby acts as an antagonist of calcineurin inhibition. We have solved the X-ray structure of unliganded FKBP12 and of FKBP12 in complex with FK506 and with rapamycin; these structures show localized differences in conformation and mobility in those regions of the protein that are known, by site-directed mutagenesis, to be involved in calcineurin inhibition. A comparison of 16 additional X-ray structures of FKBP12 in complex with FKBP12-binding ligands, where those structures were determined from different crystal forms with distinct packing arrangements, lends significance to the observed structural variability and suggests that it represents an intrinsic functional characteristic of the protein. Similar differences have been observed for FKBP12 before, but were considered artifacts of crystal-packing interactions. We suggest that immunosuppressive ligands express their differential effects in part by modulating the conformation of FKBP12, in agreement with mutagenesis experiments on the protein, and not simply through differences in the ligand structures themselves.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299838}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299838 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299838}}
 ==About this Structure==
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 [[Category: Fk506 binding protein]]
 [[Category: Fkbp12]]
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