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- SASDBP9: Human Hsp90 co-chaperone Cdc37 protein (CD37) (Hsp90 co-chaperone... -

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Basic information

Entry
Database: SASBDB / ID: SASDBP9
SampleHuman Hsp90 co-chaperone Cdc37 protein (CD37)
  • Hsp90 co-chaperone Cdc37 (protein), CDC37, Homo sapiens
Function / homology
Function and homology information


regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of mitophagy in response to mitochondrial depolarization / protein kinase regulator activity / protein folding chaperone complex / post-transcriptional regulation of gene expression / 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 ...regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of mitophagy in response to mitochondrial depolarization / protein kinase regulator activity / protein folding chaperone complex / post-transcriptional regulation of gene expression / 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 cyclin-dependent protein serine/threonine kinase activity / regulation of type I interferon-mediated signaling pathway / protein targeting / RHOBTB2 GTPase cycle / Signaling by ERBB2 / heat shock protein binding / Constitutive Signaling by Overexpressed ERBB2 / Signaling by ERBB2 TMD/JMD mutants / Hsp90 protein binding / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / Regulation of necroptotic cell death / Downregulation of ERBB2 signaling / kinase binding / unfolded protein binding / protein folding / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / protein-folding chaperone binding / scaffold protein binding / protein stabilization / protein kinase binding / extracellular exosome / cytosol / cytoplasm
Similarity search - Function
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
Similarity search - Domain/homology
Hsp90 co-chaperone Cdc37
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationDate: 2018 Mar
Title: Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System
Authors: Bunney T / Inglis A / Sanfelice D / Farrell B / Kerr C / Thompson G / Masson G / Thiyagarajan N / Svergun D / Williams R / Breeze A
Contact author
  • Chris Kerr (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #1123
Type: mix / Software: (ATSAS2.7.2) / Radius of dummy atoms: 1.90 A / Chi-square value: 1.88
Search similar-shape structures of this assembly by Omokage search (details)
Model #1124
Type: dummy / Software: (ATSAS2.7.2) / Radius of dummy atoms: 3.00 A / Symmetry: P1 / Chi-square value: 1.635
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Human Hsp90 co-chaperone Cdc37 protein (CD37) / Specimen concentration: 1.10-4.20
BufferName: 25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP
pH: 8
Entity #585Name: CDC37 / Type: protein / Description: Hsp90 co-chaperone Cdc37 / Formula weight: 44.426 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q16543
Sequence: MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD ...Sequence:
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDGSV

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Human Hsp90 co-chaperone Cdc37 protein (CD37) / Measurement date: Jul 10, 2016 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 0.045 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0248 5.0307
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1786 /
MinMax
Q0.0909164 5.00866
P(R) point1 1786
R0 15.53
Result
Type of curve: extrapolated
ExperimentalStandardStandard errorPorod
MW49.1 kDa49.1 kDa5 52 kDa
Volume---106.46 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I06042 18.03 5968.74 17.13
Radius of gyration, Rg4.19 nm0.02 3.99 nm0.59

MinMaxError
D-15.53 3
Guinier point25 110 -

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