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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-31340 | |||||||||
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| Title | Fzd7 -Gs complex | |||||||||
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Sample |
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Keywords | GPCR / Class F / Frizzled / Fzd7 / Frizzled 7 / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationnegative regulation of ectodermal cell fate specification / guanyl nucleotide binding / negative regulation of cardiac muscle cell differentiation / somatic stem cell division / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / Wnt receptor activity / non-canonical Wnt signaling pathway / mesenchymal to epithelial transition / positive regulation of epithelial cell proliferation involved in wound healing / Wnt-protein binding ...negative regulation of ectodermal cell fate specification / guanyl nucleotide binding / negative regulation of cardiac muscle cell differentiation / somatic stem cell division / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / Wnt receptor activity / non-canonical Wnt signaling pathway / mesenchymal to epithelial transition / positive regulation of epithelial cell proliferation involved in wound healing / Wnt-protein binding / WNT5:FZD7-mediated leishmania damping / frizzled binding / PCP/CE pathway / Class B/2 (Secretin family receptors) / regulation of canonical Wnt signaling pathway / Wnt signaling pathway, planar cell polarity pathway / stem cell population maintenance / PKA activation in glucagon signalling / positive regulation of phosphorylation / negative regulation of cell-substrate adhesion / developmental growth / hair follicle placode formation / canonical Wnt signaling pathway / D1 dopamine receptor binding / intracellular transport / vascular endothelial cell response to laminar fluid shear stress / renal water homeostasis / activation of adenylate cyclase activity / Hedgehog 'off' state / adenylate cyclase-activating adrenergic receptor signaling pathway / cellular response to retinoic acid / phosphatidylinositol-4,5-bisphosphate binding / cellular response to glucagon stimulus / regulation of insulin secretion / substrate adhesion-dependent cell spreading / adenylate cyclase activator activity / trans-Golgi network membrane / Asymmetric localization of PCP proteins / positive regulation of JNK cascade / PDZ domain binding / negative regulation of inflammatory response to antigenic stimulus / G protein-coupled receptor activity / bone development / platelet aggregation / G-protein beta/gamma-subunit complex binding / cognition / Olfactory Signaling Pathway / Activation of the phototransduction cascade / adenylate cyclase-activating G protein-coupled receptor signaling pathway / recycling endosome membrane / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / neuron differentiation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / photoreceptor disc membrane / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / sensory perception of smell / cellular response to catecholamine stimulus / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / T cell differentiation in thymus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / sensory perception of taste / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / positive regulation of cold-induced thermogenesis / retina development in camera-type eye / G protein activity / GTPase binding / Ca2+ pathway / fibroblast proliferation / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.22 Å | |||||||||
Authors | Chen B / Xu L | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell Res / Year: 2021Title: Cryo-EM structure of constitutively active human Frizzled 7 in complex with heterotrimeric G. Authors: Lu Xu / Bo Chen / Hannes Schihada / Shane C Wright / Ainoleena Turku / Yiran Wu / Gye-Won Han / Maria Kowalski-Jahn / Pawel Kozielewicz / Carl-Fredrik Bowin / Xianjun Zhang / Chao Li / ...Authors: Lu Xu / Bo Chen / Hannes Schihada / Shane C Wright / Ainoleena Turku / Yiran Wu / Gye-Won Han / Maria Kowalski-Jahn / Pawel Kozielewicz / Carl-Fredrik Bowin / Xianjun Zhang / Chao Li / Michel Bouvier / Gunnar Schulte / Fei Xu / ![]() | |||||||||
| History |
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_31340.map.gz | 1.9 MB | EMDB map data format | |
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| Header (meta data) | emd-31340-v30.xml emd-31340.xml | 14.8 KB 14.8 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_31340_fsc.xml | 6.9 KB | Display | FSC data file |
| Images | emd_31340.png | 30.1 KB | ||
| Filedesc metadata | emd-31340.cif.gz | 6.2 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31340 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31340 | HTTPS FTP |
-Validation report
| Summary document | emd_31340_validation.pdf.gz | 410.5 KB | Display | EMDB validaton report |
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| Full document | emd_31340_full_validation.pdf.gz | 410 KB | Display | |
| Data in XML | emd_31340_validation.xml.gz | 9.2 KB | Display | |
| Data in CIF | emd_31340_validation.cif.gz | 11.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31340 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31340 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8yy8MC ![]() 9ew2M ![]() 7evw M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_31340.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : human Frizzled 7 in complex with heterotrimeric Gs
| Entire | Name: human Frizzled 7 in complex with heterotrimeric Gs |
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| Components |
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-Supramolecule #1: human Frizzled 7 in complex with heterotrimeric Gs
| Supramolecule | Name: human Frizzled 7 in complex with heterotrimeric Gs / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: minGas
| Macromolecule | Name: minGas / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 28.907684 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: NSKTEDQRNE EKAQREANKK IEKQLQKDKQ VYRATHRLLL LGADNSGKST IVKQMRILHG GSGGSGGTSG IFETKFQVDK VNFHMFDVG GQRDERRKWI QCFNDVTAII FVVDSSDYNR LQEALNLFKS IWNNRWLRTI SVILFLNKQD LLAEKVLAGK S KIEDYFPE ...String: NSKTEDQRNE EKAQREANKK IEKQLQKDKQ VYRATHRLLL LGADNSGKST IVKQMRILHG GSGGSGGTSG IFETKFQVDK VNFHMFDVG GQRDERRKWI QCFNDVTAII FVVDSSDYNR LQEALNLFKS IWNNRWLRTI SVILFLNKQD LLAEKVLAGK S KIEDYFPE FARYTTPEDA TPEPGEDPRV TRAKYFIRDE FLRISTASGD GRHYCYPHFT CAVDTENARR IFNDCRDIIQ RM HLRQYEL L |
-Macromolecule #2: Ggamma
| Macromolecule | Name: Ggamma / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 10.366764 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: HHHHHHGGGS DSLEFIASKL AGGGSMASNN TASIAQARKL VEQLKMEANI DRIKVSKAAA DLMAYCEAHA KEDPLLTPVP ASENPFREK KFFSAIL |
-Macromolecule #3: Nb35
| Macromolecule | Name: Nb35 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 16.054232 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKYLLPTAAA GLLLLAAQPA MAMQVQLQES GGGLVQPGGS LRLSCAASGF TFSNYKMNWV RQAPGKGLEW VSDISQSGAS ISYTGSVKG RFTISRDNAK NTLYLQMNSL KPEDTAVYYC ARCPAPFTRD CFDVTSTTYA YRGQGTQVTV |
-Macromolecule #4: Frizzled-7
| Macromolecule | Name: Frizzled-7 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 67.137562 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: AAAAAAAAAA AAAMKTIIAL SYIFCLVFAD YKDDDDKEKG ISVPDHGFCQ PISIPLCTDI AYNQTILPNL LGHTNQEDAG LEVHQFYPL VKVQCSPELR FFLCSMYAPV CTVLDQAIPP CRSLCERARQ GCEALMNKFG FQWPERLRCE NFPVHGAGEI C VGQNTSDG ...String: AAAAAAAAAA AAAMKTIIAL SYIFCLVFAD YKDDDDKEKG ISVPDHGFCQ PISIPLCTDI AYNQTILPNL LGHTNQEDAG LEVHQFYPL VKVQCSPELR FFLCSMYAPV CTVLDQAIPP CRSLCERARQ GCEALMNKFG FQWPERLRCE NFPVHGAGEI C VGQNTSDG SGGPGGGPTA YPTAPYLPDL PFTALPPGAS DGRGRPAFPF SCPRQLKVPP YLGYRFLGER DCGAPCEPGR AN GLMYFKE EERRFARLWV GVWSVLCCAS TLFTVLTYLV DMRRFSYPER PIIFLSGCYF MVAVAHVAGF LLEDRAVCVE RFS DDGYRT VAQGTKKEGC TILFMVLYFF GMASSIWWVI LSLTWFLAAG MKWGHEAIEA NSQYFHLAAW AVPAVKTITI LAMG QVDGD LLSGVCYVGL SSVDALRGFV LAPLFVYLFI GTSFLLAGFV SLFRIRTIMK HDGTKTEKLE KLMVRIGVFS VLYTV PATI VLACYFYEQA FREHWERTWL LQTCKSYAVP CPPGHFPPMS PDFTVFMIKY LMTMIVGITT GFWIWSGKTL QSWRRF YHR LSHSSKGETA VHHHHHHHHH HGLNDIFEAQ KIEWHE UniProtKB: Frizzled-7 |
-Macromolecule #5: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
| Macromolecule | Name: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 37.41693 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC RFLDDNQIVT S SGDTTCAL ...String: MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC RFLDDNQIVT S SGDTTCAL WDIETGQQTT TFTGHTGDVM SLSLAPDTRL FVSGACDASA KLWDVREGMC RQTFTGHESD INAICFFPNG NA FATGSDD ATCRLFDLRA DQELMTYSHD NIICGITSVS FSKSGRLLLA GYDDFNCNVW DALKADRAGV LAGHDNRVSC LGV TDDGMA VATGSWDSFL KIWN UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 1.5 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal magnification: 130000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation

UCSF Chimera


































Z (Sec.)
Y (Row.)
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