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- PDB-2k5b: Human CDC37-HSP90 docking model based on NMR -

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Basic information

Entry
Database: PDB / ID: 2k5b
TitleHuman CDC37-HSP90 docking model based on NMR
Components
  • Heat shock protein HSP 90-alpha
  • Hsp90 co-chaperone Cdc37
KeywordsCHAPERONE / CDC37 / HSP90 / protein-protein interaction / heat shock protein / P50 / Alternative splicing / ATP-binding / Cytoplasm / Nucleotide-binding / Phosphoprotein / Stress response / Polymorphism
Function / homology
Function and homology information


regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of type 2 mitophagy / protein kinase regulator activity / protein folding chaperone complex / regulation of cyclin-dependent protein serine/threonine kinase activity / sperm mitochondrial sheath / sulfonylurea receptor binding / dATP binding / CTP binding ...regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of type 2 mitophagy / protein kinase regulator activity / protein folding chaperone complex / regulation of cyclin-dependent protein serine/threonine kinase activity / sperm mitochondrial sheath / sulfonylurea receptor binding / dATP binding / CTP binding / post-transcriptional regulation of gene expression / positive regulation of protein polymerization / vRNP Assembly / Scavenging by Class F Receptors / UTP binding / sperm plasma membrane / chaperone-mediated autophagy / Rho GDP-dissociation inhibitor binding / Respiratory syncytial virus genome replication / telomerase holoenzyme complex assembly / mitochondrial transport / Uptake and function of diphtheria toxin / protein insertion into mitochondrial outer membrane / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / regulation of type I interferon-mediated signaling pathway / TPR domain binding / PIWI-interacting RNA (piRNA) biogenesis / Assembly and release of respiratory syncytial virus (RSV) virions / non-chaperonin molecular chaperone ATPase / dendritic growth cone / Sema3A PAK dependent Axon repulsion / protein unfolding / positive regulation of cell size / regulation of protein ubiquitination / HSF1-dependent transactivation / response to unfolded protein / enzyme-substrate adaptor activity / skeletal muscle contraction / regulation of postsynaptic membrane neurotransmitter receptor levels / regulation of protein-containing complex assembly / HSF1 activation / telomere maintenance via telomerase / Attenuation phase / chaperone-mediated protein complex assembly / protein targeting / neurofibrillary tangle assembly / axonal growth cone / RHOBTB2 GTPase cycle / positive regulation of lamellipodium assembly / eNOS activation / nitric oxide metabolic process / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / DNA polymerase binding / heat shock protein binding / positive regulation of defense response to virus by host / response to salt stress / Signaling by ERBB2 / cardiac muscle cell apoptotic process / positive regulation of telomere maintenance via telomerase / endocytic vesicle lumen / positive regulation of cardiac muscle contraction / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / nitric-oxide synthase regulator activity / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / activation of innate immune response / Anchoring of the basal body to the plasma membrane / lysosomal lumen / positive regulation of interferon-beta production / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / response to cold / ESR-mediated signaling / Constitutive Signaling by Overexpressed ERBB2 / protein tyrosine kinase binding / AURKA Activation by TPX2 / VEGFR2 mediated vascular permeability / Hsp90 protein binding / ATP-dependent protein folding chaperone / response to cocaine / Signaling by ERBB2 TMD/JMD mutants / brush border membrane / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / DDX58/IFIH1-mediated induction of interferon-alpha/beta / cellular response to virus / Regulation of actin dynamics for phagocytic cup formation / Regulation of necroptotic cell death / tau protein binding / VEGFA-VEGFR2 Pathway
Similarity search - Function
Cdc37, Hsp90 binding domain / Cdc37, C-terminal / Cdc37, Hsp90 binding / Cdc37, Hsp90-binding domain superfamily / Cdc37 C terminal domain / Cdc37 Hsp90 binding domain / Cdc37 C terminal domain / Cdc37 Hsp90 binding domain / Cdc37 N terminal kinase binding / Cdc37 ...Cdc37, Hsp90 binding domain / Cdc37, C-terminal / Cdc37, Hsp90 binding / Cdc37, Hsp90-binding domain superfamily / Cdc37 C terminal domain / Cdc37 Hsp90 binding domain / Cdc37 C terminal domain / Cdc37 Hsp90 binding domain / Cdc37 N terminal kinase binding / Cdc37 / Cdc37, N-terminal domain / Cdc37 N terminal kinase binding / Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-like ATPase, C-terminal domain / Heat Shock Protein 90 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Heat shock protein HSP 90-alpha / Hsp90 co-chaperone Cdc37
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
Model detailsStructure of the human CDC37-HSP90 complex based on NMR using CSPs, RDCs and docking with HADDOCK
AuthorsSreeramulu, S. / Jonker, H.R.A. / Lancaster, C.R. / Richter, C. / Langer, T. / Schwalbe, H.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy
Authors: Sreeramulu, S. / Jonker, H.R.A. / Langer, T. / Richter, C. / Lancaster, C.R. / Schwalbe, H.
History
DepositionJun 26, 2008Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Dec 9, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Heat shock protein HSP 90-alpha
B: Hsp90 co-chaperone Cdc37


Theoretical massNumber of molelcules
Total (without water)39,0572
Polymers39,0572
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200structures with the best HADDOCK scoring
RepresentativeModel #1best haddock score

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Components

#1: Protein Heat shock protein HSP 90-alpha / HSP 86 / Renal carcinoma antigen NY-REN-38


Mass: 23535.592 Da / Num. of mol.: 1 / Fragment: residues 14-223
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HSP90AA1, HSP90A, HSPC1, HSPCA / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P07900
#2: Protein Hsp90 co-chaperone Cdc37 / Hsp90 chaperone protein kinase-targeting subunit / p50Cdc37


Mass: 15521.082 Da / Num. of mol.: 1 / Fragment: residues 148-276
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDC37, CDC37A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q16543
Sequence detailsTHIS RESIDUE IS UNP DATABASE P07900 REF.1(CAA33259)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
Details: Structure of the human CDC37-HSP90 complex based on NMR using CSPs, RDCs and docking with HADDOCK
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1223D 1H-15N NOESY
1333D 1H-15N NOESY
141IPAP(1H,15N)HSQC
151IPAP(1H,15N)HSQC

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Sample preparation

Details
Solution-IDContentsSolvent system
10.8mM [U-100% 15N] human HSP90, 0.8mM [U-100% 15N] human CDC37, 50mM HEPES, 100mM sodium chloride, 1mM DTT, 90% H2O/10% D2O90% H2O/10% D2O
20.8mM [U-100% 15N, U-100% 2H] human HSP90, 0.8mM human CDC37, 50mM HEPES, 100mM sodium chloride, 1mM DTT, 90% H2O/10% D2O90% H2O/10% D2O
30.8mM human HSP90, 0.8mM [U-100% 15N, U-100% 2H] human CDC37, 50mM HEPES, 100mM sodium chloride, 1mM DTT, 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.8 mMhuman HSP90[U-100% 15N]1
0.8 mMhuman CDC37[U-100% 15N]1
50 mMHEPES1
100 mMsodium chloride1
1 mMDTT1
0.8 mMhuman HSP90[U-100% 15N, U-100% 2H]2
0.8 mMhuman CDC372
50 mMHEPES2
100 mMsodium chloride2
1 mMDTT2
0.8 mMhuman HSP903
0.8 mMhuman CDC37[U-100% 15N, U-100% 2H]3
50 mMHEPES3
100 mMsodium chloride3
1 mMDTT3
Sample conditionsIonic strength: 100 / pH: 7.4 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE9001
Bruker AvanceBrukerAVANCE8002
Bruker AvanceBrukerAVANCE7003

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Processing

NMR software
NameVersionDeveloperClassification
TopSpin2.1Bruker Biospincollection
TopSpin2.1Bruker Biospinprocessing
Sparky3.113Goddarddata analysis
Sparky3.113Goddardpeak picking
CARA1.8.3Keller and Wuthrichdata analysis
CARA1.8.3Keller and Wuthrichpeak picking
CNS1.1Brunger, Adams, Clore, Gros, Nilges and Readstructure solution
CNS1.1Brunger, Adams, Clore, Gros, Nilges and Readrefinement
HADDOCK2A. Bonvin & C. Dominguezgeometry optimization
HADDOCK2Dominguez, Boelens and Bonvinrefinement
HADDOCK2A. Bonvin & C. Dominguezstructure solution
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1
Details: The structure was calculated using HADDOCK Details can be found in the jrnl citation above
NMR representativeSelection criteria: best haddock score
NMR ensembleConformer selection criteria: structures with the best HADDOCK scoring
Conformers calculated total number: 200 / Conformers submitted total number: 10 / Representative conformer: 1

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