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Yorodumi- PDB-1fks: SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK... -
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-Basic information
Entry | Database: PDB / ID: 1fks | ||||||
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Title | SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN | ||||||
Components | FK506 AND RAPAMYCIN-BINDING PROTEIN | ||||||
Keywords | CIS-TRANS ISOMERASE | ||||||
Function / homology | Function and homology information macrolide binding / activin receptor binding / cytoplasmic side of membrane / transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / signaling receptor inhibitor activity / type I transforming growth factor beta receptor binding / negative regulation of activin receptor signaling pathway / regulation of amyloid precursor protein catabolic process / heart trabecula formation ...macrolide binding / activin receptor binding / cytoplasmic side of membrane / transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / signaling receptor inhibitor activity / type I transforming growth factor beta receptor binding / negative regulation of activin receptor signaling pathway / regulation of amyloid precursor protein catabolic process / heart trabecula formation / terminal cisterna / ryanodine receptor complex / I-SMAD binding / protein maturation by protein folding / 'de novo' protein folding / ventricular cardiac muscle tissue morphogenesis / negative regulation of phosphoprotein phosphatase activity / FK506 binding / mTORC1-mediated signalling / TGF-beta receptor signaling activates SMADs / Calcineurin activates NFAT / regulation of immune response / protein peptidyl-prolyl isomerization / supramolecular fiber organization / heart morphogenesis / regulation of ryanodine-sensitive calcium-release channel activity / sarcoplasmic reticulum membrane / T cell activation / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / sarcoplasmic reticulum / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / calcium ion transmembrane transport / negative regulation of transforming growth factor beta receptor signaling pathway / Z disc / SARS-CoV-1 activates/modulates innate immune responses / regulation of protein localization / protein folding / positive regulation of protein binding / protein refolding / positive regulation of canonical NF-kappaB signal transduction / amyloid fibril formation / Potential therapeutics for SARS / transmembrane transporter binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Michnick, S.W. / Rosen, M.K. / Wandless, T.J. / Karplus, M. / Schreiber, S.L. | ||||||
Citation | Journal: Science / Year: 1991 Title: Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Authors: Michnick, S.W. / Rosen, M.K. / Wandless, T.J. / Karplus, M. / Schreiber, S.L. #1: Journal: Biochemistry / Year: 1991 Title: Proton and Nitrogen Sequential Assignments and Secondary Structure Determination of the Human Fk506 and Rapamycin Binding Protein Authors: Rosen, M.K. / Michnick, S.W. / Karplus, M. / Schreiber, S.L. #2: Journal: Nature / Year: 1990 Title: Molecular Cloning and Overexpression of the Human Fk506-Binding Protein Fkbp Authors: Standaert, R.F. / Galat, A. / Verdine, G.L. / Schreiber, S.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fks.cif.gz | 42.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fks.ent.gz | 33.4 KB | Display | PDB format |
PDBx/mmJSON format | 1fks.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fk/1fks ftp://data.pdbj.org/pub/pdb/validation_reports/fk/1fks | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: THE LIGAND BINDING SITE IS LINED BY A NUMBER OF CONSERVED AROMATIC AND ALIPHATIC RESIDUES. THESE ARE TYR 26, PHE 36, PHE 46, VAL 55, ILE 56, TRP 59, TYR 82 AND PHE 99. 2: THE +3, +1, -3, +1 TOPOLOGY OF THE FKBP12 BETA-SHEET RESULTS IN A CROSSING OF TWO STRAND-CONNECTING LOOPS (PRO 9 TO GLN 20, AND MET 66 TO GLN 70). TO THE BEST OF OUR KNOWLEDGE, THIS WAS THE FIRST ...2: THE +3, +1, -3, +1 TOPOLOGY OF THE FKBP12 BETA-SHEET RESULTS IN A CROSSING OF TWO STRAND-CONNECTING LOOPS (PRO 9 TO GLN 20, AND MET 66 TO GLN 70). TO THE BEST OF OUR KNOWLEDGE, THIS WAS THE FIRST EXAMPLE OF SUCH A STRUCTURE. INTERESTINGLY, THE RECENTLY-REPORTED STRUCTURE OF ANOTHER IMMUNOPHILIN (IMMUNO-SUPPRESSANT-BINDING PROTEIN), CYCLOPHILIN, ALSO CONTAINS THIS TYPE OF TOPOLOGICAL CROSSING OF TWO STRAND-CONNECTING LOOPS. THE SIGNIFICANCE OF THIS SIMILARITY, IF ANY, REMAINS UNKNOWN. 3: THE LOOPS FROM SER 39 TO LYS 44, AND ALA 83 TO HIS 94 ARE UNDERDETERMINED IN COMPARISON TO THE REMAINDER OF THE STRUCTURE. IN THE CRYSTAL STRUCTURES OF THE FKBP12-FK506 AND FKBP12-RAPAMYCIN ...3: THE LOOPS FROM SER 39 TO LYS 44, AND ALA 83 TO HIS 94 ARE UNDERDETERMINED IN COMPARISON TO THE REMAINDER OF THE STRUCTURE. IN THE CRYSTAL STRUCTURES OF THE FKBP12-FK506 AND FKBP12-RAPAMYCIN COMPLEXES, THE LATTER LOOP IS WELL DEFINED, AND MAKES NUMEROUS CONTACTS TO THE BOUND LIGANDS. WE ARE CURRENTLY IN THE PROCESS OF PERFORMING HETERONUCLEAR NOE AND RELAXATION EXPERIMENTS TO ANALYZE THE CHANGES IN MOBILITY OF THIS REGION UPON LIGAND-BINDING. | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 11836.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: S2 / References: UniProt: P62942 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 1 |