|Entry||Database: PDB / ID: 2bug|
|Title||Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide|
|Keywords||HYDROLASE / TETRATRICOPEPTIDE DOMAIN / PROTEIN PHOSPHATASE / HSP90 BINDING / IRON / MANGANESE / METAL-BINDING|
|Function / homology|
Function and homology information
Signaling by ERBB2 / Regulation of PLK1 Activity at G2/M Transition / eNOS activation / Regulation of actin dynamics for phagocytic cup formation / vRNP Assembly / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Scavenging by Class F Receptors / HSP90 chaperone cycle for steroid hormone receptors (SHR) / HSF1 activation ...Signaling by ERBB2 / Regulation of PLK1 Activity at G2/M Transition / eNOS activation / Regulation of actin dynamics for phagocytic cup formation / vRNP Assembly / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Scavenging by Class F Receptors / HSP90 chaperone cycle for steroid hormone receptors (SHR) / HSF1 activation / Anchoring of the basal body to the plasma membrane / Chaperone Mediated Autophagy / Estrogen-dependent gene expression / Extra-nuclear estrogen signaling / ESR-mediated signaling / Downregulation of ERBB2 signaling / AURKA Activation by TPX2 / The role of GTSE1 in G2/M progression after G2 checkpoint / Neutrophil degranulation / Interleukin-4 and Interleukin-13 signaling / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Negative regulation of MAPK pathway / Attenuation phase / Constitutive Signaling by EGFRvIII / PIWI-interacting RNA (piRNA) biogenesis / Recruitment of mitotic centrosome proteins and complexes / VEGFR2 mediated vascular permeability / VEGFA-VEGFR2 Pathway / HSF1-dependent transactivation / Sema3A PAK dependent Axon repulsion / Uptake and function of diphtheria toxin / Loss of Nlp from mitotic centrosomes / Recruitment of NuMA to mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / response to arachidonic acid / histone dephosphorylation / proximal dendrite / positive regulation of glucocorticoid receptor signaling pathway / peptidyl-threonine dephosphorylation / peptidyl-serine dephosphorylation / chaperone complex / protein-serine/threonine phosphatase / positive regulation of protein polymerization / protein insertion into mitochondrial outer membrane / G-protein alpha-subunit binding / protein serine/threonine phosphatase activity / telomerase holoenzyme complex assembly / response to morphine / mitochondrial transport / chaperone-mediated autophagy / positive regulation of cellular protein catabolic process / central nervous system neuron axonogenesis / TPR domain binding / phosphatase activity / dendritic growth cone / phosphoprotein phosphatase activity / chaperone-mediated protein complex assembly / telomere maintenance via telomerase / axon extension / protein unfolding / regulation of protein ubiquitination / DNA polymerase binding / regulation of protein complex assembly / regulation of cellular protein localization / cofactor metabolic process / positive regulation of tau-protein kinase activity / MHC class II protein complex binding / GTPase binding / protein tyrosine kinase binding / axonal growth cone / ADP binding / endocytic vesicle lumen / establishment of cell polarity / ciliary basal body-plasma membrane docking / response to unfolded protein / protein folding chaperone / protein heterooligomerization / regulation of nitric-oxide synthase activity / negative regulation of protein phosphorylation / response to cold / lysosomal lumen / positive regulation of telomerase activity / ATPase activity, coupled / nitric-oxide synthase regulator activity / negative regulation of neuron death / Hsp90 protein binding / protein dephosphorylation / ERBB2 signaling pathway / tau protein binding / cellular response to cadmium ion / regulation of cellular response to heat / response to lead ion / cellular response to hydrogen peroxide / melanosome / histone deacetylase binding / vascular endothelial growth factor receptor signaling pathway / regulation of G2/M transition of mitotic cell cycle / receptor-mediated endocytosis / Fc-gamma receptor signaling pathway involved in phagocytosis / protein refolding
Tetratricopeptide repeat / Histidine kinase/HSP90-like ATPase / Calcineurin-like phosphoesterase domain, ApaH type / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Serine/threonine protein phosphatase 5 / Tetratricopeptide-like helical domain superfamily / Tetratricopeptide repeat-containing domain / PPP domain / TPR repeat region circular profile. / Heat shock protein Hsp90, conserved site ...Tetratricopeptide repeat / Histidine kinase/HSP90-like ATPase / Calcineurin-like phosphoesterase domain, ApaH type / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Serine/threonine protein phosphatase 5 / Tetratricopeptide-like helical domain superfamily / Tetratricopeptide repeat-containing domain / PPP domain / TPR repeat region circular profile. / Heat shock protein Hsp90, conserved site / TPR repeat profile. / Heat shock hsp90 proteins family signature. / Serine/threonine specific protein phosphatases signature. / PPP5 TPR repeat region / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Tetratricopeptide repeat / Hsp90 protein / Calcineurin-like phosphoesterase / PP5, C-terminal metallophosphatase domain / HSP90, C-terminal domain / Histidine kinase/HSP90-like ATPase superfamily / Metallo-dependent phosphatase-like / Heat shock protein Hsp90, N-terminal / Ribosomal protein S5 domain 2-type fold / Heat shock protein Hsp90 family / Tetratricopeptide repeat 1
Heat shock protein HSP 90-alpha / Serine/threonine-protein phosphatase 5 / DSCR1
|Biological species||HOMO SAPIENS (human)|
|Method||SOLUTION NMR / ARIA|
|Authors||Cliff, M.J. / Harris, R. / Barford, D. / Ladbury, J.E. / Williams, M.A.|
|Citation||Journal: Structure / Year: 2006|
Title: Conformational Diversity in the Tpr Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90.
Authors: Cliff, M.J. / Harris, R. / Barford, D. / Ladbury, J.E. / Williams, M.A.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: SERINE/THREONINE PROTEIN PHOSPHATASE 5
|#1: Protein/peptide|| |
Mass: 16211.396 Da / Num. of mol.: 1 / Details: RESIDUES 19-147 WITH N-TERMINAL HIS-TAG / Fragment: TETRATRICOPEPTIDE DOMAIN, RESIDUES 19-147 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PQE31 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P53041, protein-serine/threonine phosphatase
|#2: Protein/peptide|| |
Mass: 647.695 Da / Num. of mol.: 1 / Details: N-TERMINALLY ACETYLATED / Fragment: C-TERMINAL PENTAPEPTIDE, RESIDUES 1-5 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: Q9H2A1, UniProt: P07900*PLUS
|Compound details||ENGINEERED||Sequence details||G83N MUTATION AND N-TERMINAL HIS TAG|
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: THE STRUCTURE WAS DETERMINED USING DISTANCE RESTRAINTS DETERMINED FROM 1H13C-NOESYHSQC (13C,15N- LABELLED PROTEIN) AND 1H15N-NOESYHSQC EXPERIMENTS (15N- LABELLED PROTEIN), AND ALSO HYDROGEN BOND RESTRAINTS FROM HYDROGEN EXCHANGE DATE, ANGLE RESTRAINTS DERIVED FROM CHEMICAL SHIFT DATA BY TALOS.|
|Details||Contents: 50MM MES, 5MM DTT (PH6.0) 10%D2O, 90% H2O|
Ionic strength: 55 mM / pH: 6.0 / Pressure: 1.0 atm / Temperature: 298.0 K
Manufacturer: Varian / Model: INOVA / Type: Varian INOVA
Name: ARIA / Version: 1.2
|Refinement||Method: ARIA / Software ordinal: 1 |
Details: REFINEMENT DETAILS CAN BE FOUND IN JOURNAL CITATION ABOVE
|NMR ensemble||Conformer selection criteria: LOWEST RESTRAINT ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 19|
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