SASDBQ9: Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast ...

Basic information

• Entry: Database: SASBDB / ID: SASDBQ9

Sample

Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast growth factor receptor 3

• Hsp90 co-chaperone Cdc37 (protein), CDC37, Homo sapiens
• Fibroblast growth factor receptor 3 (protein), FGFR3Fibroblast growth factor receptor 3, Homo sapiens

Function / homology

Function:

fibroblast growth factor receptor apoptotic signaling pathway / t(4;14) translocations of FGFR3 / negative regulation of developmental growth / Signaling by FGFR3 fusions in cancer / bone maturation / regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / chondrocyte proliferation / endochondral bone growth / positive regulation of mitophagy in response to mitochondrial depolarization / FGFR3b ligand binding and activation / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / fibroblast growth factor receptor activity / protein kinase regulator activity / endochondral ossification / positive regulation of phospholipase activity / protein folding chaperone complex / bone morphogenesis / post-transcriptional regulation of gene expression / PI-3K cascade:FGFR3 / 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 / fibroblast growth factor binding / bone mineralization / regulation of cyclin-dependent protein serine/threonine kinase activity / cell surface receptor signaling pathway via JAK-STAT / regulation of type I interferon-mediated signaling pathway / PI3K Cascade / protein targeting / fibroblast growth factor receptor signaling pathway / chondrocyte differentiation / RHOBTB2 GTPase cycle / SHC-mediated cascade:FGFR3 / FRS-mediated FGFR3 signaling / positive regulation of tyrosine phosphorylation of STAT protein / transport vesicle / Signaling by ERBB2 / Signaling by FGFR3 in disease / heat shock protein binding / Constitutive Signaling by Overexpressed ERBB2 / skeletal system development / Negative regulation of FGFR3 signaling / 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 / receptor protein-tyrosine kinase / Downregulation of ERBB2 signaling / kinase binding / cell surface receptor protein tyrosine kinase signaling pathway / Constitutive Signaling by Aberrant PI3K in Cancer / MAPK cascade / unfolded protein binding / protein folding / cell-cell signaling / PIP3 activates AKT signaling / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein-folding chaperone binding / RAF/MAP kinase cascade / scaffold protein binding / protein tyrosine kinase activity / positive regulation of MAPK cascade / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein stabilization / receptor complex / phosphorylation / positive regulation of cell population proliferation / protein kinase binding / Golgi apparatus / cell surface / endoplasmic reticulum / extracellular exosome / extracellular region / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm

Domain/homology:

Fibroblast growth factor receptor 3 transmembrane 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 / Fibroblast growth factor receptor family / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily

Component:

Fibroblast growth factor receptor 3 / Hsp90 co-chaperone Cdc37

• Biological species: Homo sapiens (human)
• Citation: Date: 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)

Models

• Model #1132: ; Type: mix / Software: (ATSAS2.7.2) / Radius of dummy atoms: 3.50 A / Symmetry: P1 / Chi-square value: 2.17; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1133: ; Type: dummy / Software: (ATSAS2.7.2) / Radius of dummy atoms: 3.00 A / Symmetry: P1 / Chi-square value: 1.443; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast growth factor receptor 3; Specimen concentration: 1.00-3.80 / Entity id: 585 / 589
• Buffer: Name: 25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP; pH: 8

Entity #585

Name: 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 SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDGSV

Entity #589

Name: FGFR3Fibroblast growth factor receptor 3 / Type: protein / Description: Fibroblast growth factor receptor 3 / Formula weight: 35.478 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P22607
Sequence:

SELELPADPK WELSRARLTL GKPLGEGAFG QVVMAEAIGI DKDRAAKPVT VAVKMLKDDA TDKDLSDLVS EMEMMKMIGK HKNFINLLGA CTQGGPLYVL VEYAAKGNLR EFLRARRPPG LDYSFDTSKP PEEQLTFKDL VSCAYQVARG MEYLASQKCI HRDLAARNVL VTEDNVMKIA DFGLARDVHN LDYYKKTTNG RLPVKWMAPE ALFDRVYTHQ SDVWSFGVLL WEIFTLGGSP YPGIPVEELF KLLKEGHRMD KPANCTHDLY MIMRECWHAA PSQRPTFKQL VEDLDRVLTV TSTDEYLDLS APFE

Experimental information

• Beam: Instrument 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
• Detector: Name: Pilatus 2M

Scan

Title: Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast growth factor receptor 3
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 /

	Min	Max
Q	0.0248	5.0307

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 1780 /

	Min	Max
Q	0.129487	5.0307
P(R) point	1	1780
R	0	19.47

Result

Type of curve: extrapolated

	Experimental	Standard	Standard error	Porod
MW	76.7 kDa	76.7 kDa	8	99 kDa
Volume	-	-	-	161.47 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	9427	49.97	9320.76	67.41
Radius of gyration, Rg	4.967 nm	0.044	4.69 nm	0.19

	Min	Max	Error
D	-	19.47	5
Guinier point	39	92	-