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), FGFR3, Homo sapiens

Function / homology

Function:

t(4;14) translocations of FGFR3 / negative regulation of developmental growth / fibroblast growth factor receptor apoptotic signaling pathway / 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 / FGFR3b ligand binding and activation / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / endochondral ossification / positive regulation of phospholipase activity / positive regulation of type 2 mitophagy / bone morphogenesis / protein kinase regulator activity / protein folding chaperone complex / regulation of cyclin-dependent protein serine/threonine kinase activity / positive regulation of tyrosine phosphorylation of STAT protein / PI-3K cascade:FGFR3 / post-transcriptional regulation of gene expression / bone mineralization / 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 / fibroblast growth factor binding / PI3K Cascade / cell surface receptor signaling pathway via JAK-STAT / fibroblast growth factor receptor signaling pathway / chondrocyte differentiation / SHC-mediated cascade:FGFR3 / protein targeting / RHOBTB2 GTPase cycle / transport vesicle / FRS-mediated FGFR3 signaling / Signaling by FGFR3 in disease / heat shock protein binding / Signaling by ERBB2 / Constitutive Signaling by Overexpressed ERBB2 / skeletal system development / Negative regulation of FGFR3 signaling / Hsp90 protein binding / Signaling by ERBB2 TMD/JMD mutants / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / Constitutive Signaling by EGFRvIII / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / Signaling by ERBB2 ECD mutants / receptor protein-tyrosine kinase / Signaling by ERBB2 KD Mutants / Regulation of necroptotic cell death / kinase binding / Downregulation of ERBB2 signaling / 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 / protein-folding chaperone binding / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein tyrosine kinase activity / scaffold protein binding / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / positive regulation of ERK1 and ERK2 cascade / positive regulation of MAPK cascade / protein stabilization / positive regulation of cell population proliferation / protein kinase binding / cell surface / endoplasmic reticulum / Golgi apparatus / extracellular exosome / extracellular region

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. / Tyrosine-protein kinase, active site / Immunoglobulin subtype / Immunoglobulin / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / 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: FGFR3 / 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 synchrotron / 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	-