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- PDB-1f40: SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROP... -
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Basic information
Entry | Database: PDB / ID: 1f40 | ||||||
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Title | SOLUTION STRUCTURE OF FKBP12 COMPLEXED WITH GPI-1046, A NEUROTROPHIC LIGAND | ||||||
![]() | FK506 BINDING PROTEIN (FKBP12) | ||||||
![]() | ISOMERASE | ||||||
Function / homology | ![]() macrolide binding / activin receptor binding / cytoplasmic side of membrane / signaling receptor inhibitor activity / transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / type I transforming growth factor beta receptor binding / negative regulation of activin receptor signaling pathway / heart trabecula formation / terminal cisterna ...macrolide binding / activin receptor binding / cytoplasmic side of membrane / signaling receptor inhibitor activity / transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / type I transforming growth factor beta receptor binding / negative regulation of activin receptor signaling pathway / heart trabecula formation / terminal cisterna / ryanodine receptor complex / I-SMAD binding / regulation of amyloid precursor protein catabolic process / protein maturation by protein folding / ventricular cardiac muscle tissue morphogenesis / 'de novo' protein folding / 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 / heart morphogenesis / supramolecular fiber organization / regulation of ryanodine-sensitive calcium-release channel activity / sarcoplasmic reticulum membrane / T cell activation / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / peptidylprolyl isomerase / sarcoplasmic reticulum / 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 / transmembrane transporter binding / amyloid fibril formation / Potential therapeutics for SARS / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Sich, C. / Improta, S. / Cowley, D.J. / Guenet, C. / Merly, J.P. / Teufel, M. / Saudek, V. | ||||||
![]() | ![]() Title: Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics. Authors: Sich, C. / Improta, S. / Cowley, D.J. / Guenet, C. / Merly, J.P. / Teufel, M. / Saudek, V. #1: ![]() Title: Neurotrophic Immunophilin Ligands Stimulate Structural and Functional Recovery in Neurodegenerative Animal Models Authors: Steiner, J.P. / Hamilton, G.S. / Ross, D.T. / Valentine, H.L. / Guo, H. / Connolly, M.A. / Liang, S. / Ramsey, C. / Li, J.H. / Huang, W. / Howorth, P. / Soni, R. / Fuller, M. / Sauer, H. / ...Authors: Steiner, J.P. / Hamilton, G.S. / Ross, D.T. / Valentine, H.L. / Guo, H. / Connolly, M.A. / Liang, S. / Ramsey, C. / Li, J.H. / Huang, W. / Howorth, P. / Soni, R. / Fuller, M. / Sauer, H. / Nowotnik, A.C. / Suzdak, P.D. #2: ![]() Title: Atomic Structure of FKBP-FK506, an Immunophilin-immunosuppressant Complex Authors: van Duyne, G.D. / Staendert, R.F. / Karplus, P.A. / Schreiber, S.L. / Clardy, J. #3: ![]() Title: Design, Synthesis, and Kinetic Evaluation of high-affinity FKBP Ligands and the X-ray Structure of their Complexes with FKBP12 Authors: Holt, D.A. / Luengo, J.I. / Yamashita, D.S. / Oh, H.-J. / Konalian, A.L. / Yen, H.-K. / Rozamus, L.W. / Brandt, M. / Bossard, M.J. / Levy, M.A. / Eggleston, D.S. / Lian, J. / Schultz, L.W. / ...Authors: Holt, D.A. / Luengo, J.I. / Yamashita, D.S. / Oh, H.-J. / Konalian, A.L. / Yen, H.-K. / Rozamus, L.W. / Brandt, M. / Bossard, M.J. / Levy, M.A. / Eggleston, D.S. / Lian, J. / Schultz, L.W. / Stout, T.J. / Clardy, J. #4: ![]() Title: 15N NMR Relaxation Studies of the FK506 Binding Protein: Dynamic Effects of Ligand Binding and Implications for Calcinerin Inhibition Authors: Cheng, J.W. / Lepre, C.A. / Moore, J.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 366.2 KB | Display | ![]() |
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PDB format | ![]() | 303.3 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 440.8 KB | Display | ![]() |
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Full document | ![]() | 474.9 KB | Display | |
Data in XML | ![]() | 15.6 KB | Display | |
Data in CIF | ![]() | 27.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Similar structure data |
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Assembly
Deposited unit | ![]()
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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 Details: PROTEIN COORDINATES WERE TAKEN FROM THE CRYSTAL STRUCTURE BY HOLT ET AL. (1993, PDB ACCESSION CODE 1FKG). Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GPI / ( |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | Ionic strength: 100mM / pH: 6.5 / Pressure: ambient / Temperature: 300 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Structures were calculated using a total of 50 ligand-ligand and 18 protein-ligand distance restraints. NOEs involving degenerate protons were incorporated as ambiguous restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 10 |