1fkt
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fkr|1FKR]], [[1fks|1FKS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkt OCA], [http://www.ebi.ac.uk/pdbsum/1fkt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fkt RCSB]</span> | ||
}} | }} | ||
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[[Category: cis-trans isomerase]] | [[Category: cis-trans isomerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:24:52 2008'' |
Revision as of 17:25, 30 March 2008
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| Related: | 1FKR, 1FKS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
Overview
Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel beta-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
About this Structure
1FKT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin., Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL, Science. 1991 May 10;252(5007):836-9. PMID:1709301
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