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'''SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN''' | '''SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN''' | ||
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[[Category: Schreiber, S L.]] | [[Category: Schreiber, S L.]] | ||
[[Category: Wandless, T J.]] | [[Category: Wandless, T J.]] | ||
[[Category: | [[Category: Cis-trans isomerase]] | ||
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Revision as of 16:26, 2 May 2008
SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN
OverviewOverview
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 StructureAbout this Structure
1FKR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 16:26:41 2008