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- SASDBQ9: Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast ... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDBQ9 |
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![]() | Human Hsp90 co-chaperone Cdc37 (CD37) in complex with fibroblast growth factor receptor 3
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Function / homology | ![]() 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 ...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 / endochondral ossification / positive regulation of phospholipase activity / protein kinase regulator activity / protein folding chaperone complex / bone morphogenesis / post-transcriptional regulation of gene expression / regulation of cyclin-dependent protein serine/threonine kinase activity / 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 / PI-3K cascade:FGFR3 / fibroblast growth factor binding / bone mineralization / cell surface receptor signaling pathway via JAK-STAT / regulation of type I interferon-mediated signaling pathway / PI3K Cascade / fibroblast growth factor receptor signaling pathway / protein targeting / RHOBTB2 GTPase cycle / chondrocyte differentiation / 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 / Constitutive Signaling by Aberrant PI3K in Cancer / MAPK cascade / unfolded protein binding / protein folding / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / PIP3 activates AKT signaling / cell-cell signaling / protein-folding chaperone binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / scaffold protein binding / protein tyrosine kinase activity / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of ERK1 and ERK2 cascade / receptor complex / protein stabilization / 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 / cytoplasm / cytosol Similarity search - Function |
Biological species | ![]() |
![]() | ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #1132 | ![]() Type: mix / Software: (ATSAS2.7.2) / Radius of dummy atoms: 3.50 A / Symmetry: P1 / Chi-square value: 2.17 ![]() |
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Model #1133 | ![]() Type: dummy / Software: (ATSAS2.7.2) / Radius of dummy atoms: 3.00 A / Symmetry: P1 / Chi-square value: 1.443 ![]() |
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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 |
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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 ...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 ...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 ![]() | ||||||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | ||||||||||||||||||||||||||||||||||||||||||
Scan | 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 /
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Distance distribution function P(R) |
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Result |
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