PDBsum entry 1fkt

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Cis-trans isomerase PDB id
Protein chain
107 a.a.

References listed in PDB file
Key reference
Title Solution structure of fkbp, A rotamase enzyme and receptor for fk506 and rapamycin.
Authors S.W.Michnick, M.K.Rosen, T.J.Wandless, M.Karplus, S.L.Schreiber.
Ref. Science, 1991, 252, 836-839. [DOI no: 10.1126/science.1709301]
PubMed id 1709301
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.
Secondary reference #1
Title Proton and nitrogen sequential assignments and secondary structure determination of the human fk506 and rapamycin binding protein.
Authors M.K.Rosen, S.W.Michnick, M.Karplus, S.L.Schreiber.
Ref. Biochemistry, 1991, 30, 4774-4789. [DOI no: 10.1021/bi00233a020]
PubMed id 1709363
Full text Abstract
Secondary reference #2
Title Molecular cloning and overexpression of the human fk506-Binding protein fkbp.
Authors R.F.Standaert, A.Galat, G.L.Verdine, S.L.Schreiber.
Ref. Nature, 1990, 346, 671-674. [DOI no: 10.1038/346671a0]
PubMed id 1696686
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