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- EMDB-44642: Cholecystokinin 1 receptor (CCK1R) Y140A mutant, Gq chimera (mGsq... -
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Open data
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Basic information
Entry | ![]() | |||||||||||||||
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Title | Cholecystokinin 1 receptor (CCK1R) Y140A mutant, Gq chimera (mGsqi) complex | |||||||||||||||
![]() | best class, local refinement (micelle and ScFv16 masked out), sharpened | |||||||||||||||
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![]() | cholecystokinin / GPCR / cholesterol / mutant / MEMBRANE PROTEIN | |||||||||||||||
Function / homology | ![]() cholecystokinin receptor activity / cholecystokinin signaling pathway / regulation of hormone secretion / neuropeptide receptor activity / neuropeptide hormone activity / peptide hormone receptor binding / eating behavior / peptide hormone binding / PKA activation in glucagon signalling / hair follicle placode formation ...cholecystokinin receptor activity / cholecystokinin signaling pathway / regulation of hormone secretion / neuropeptide receptor activity / neuropeptide hormone activity / peptide hormone receptor binding / eating behavior / peptide hormone binding / PKA activation in glucagon signalling / hair follicle placode formation / mu-type opioid receptor binding / developmental growth / corticotropin-releasing hormone receptor 1 binding / intracellular transport / Adenylate cyclase inhibitory pathway / D1 dopamine receptor binding / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling / D2 dopamine receptor binding / Hedgehog 'off' state / G protein-coupled serotonin receptor binding / beta-2 adrenergic receptor binding / adenylate cyclase-activating adrenergic receptor signaling pathway / regulation of mitotic spindle organization / cellular response to forskolin / forebrain development / cellular response to hormone stimulus / digestion / activation of adenylate cyclase activity / adenylate cyclase activator activity / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / Peptide ligand-binding receptors / axonogenesis / trans-Golgi network membrane / Regulation of insulin secretion / G protein-coupled receptor binding / peptide binding / insulin-like growth factor receptor binding / ionotropic glutamate receptor binding / neuron migration / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / bone development / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G-protein activation / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / cognition / Sensory perception of sweet, bitter, and umami (glutamate) taste / response to peptide hormone / photoreceptor disc membrane / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / platelet aggregation / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / cellular response to catecholamine stimulus / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / sensory perception of taste / ADP signalling through P2Y purinoceptor 1 / adenylate cyclase-activating dopamine receptor signaling pathway / G beta:gamma signalling through PI3Kgamma / cellular response to prostaglandin E stimulus / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / GDP binding / G-protein beta-subunit binding / Inactivation, recovery and regulation of the phototransduction cascade / heterotrimeric G-protein complex / G alpha (12/13) signalling events / extracellular vesicle / sensory perception of smell / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / GTPase binding / retina development in camera-type eye / phospholipase C-activating G protein-coupled receptor signaling pathway / Ca2+ pathway / positive regulation of cold-induced thermogenesis / cell cortex / midbody / G alpha (i) signalling events / fibroblast proliferation / G alpha (s) signalling events / G alpha (q) signalling events / cell population proliferation Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.59 Å | |||||||||||||||
![]() | Cary BP / Harikumar KG / Zhao P / Desai AJ / Mobbs JM / Toufaily C / Furness SGB / Christopoulos A / Belousoff MJ / Wootten D ...Cary BP / Harikumar KG / Zhao P / Desai AJ / Mobbs JM / Toufaily C / Furness SGB / Christopoulos A / Belousoff MJ / Wootten D / Sexton PM / Miller LJ | |||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Cholesterol-dependent dynamic changes in the conformation of the type 1 cholecystokinin receptor affect ligand binding and G protein coupling Authors: Harikumar KG / Zhao P / Cary BP / Xu X / Desai AJ / Mobbs JI / Toufaily C / Furness SGB / Christopoulos A / Belousoff MJ / Wootten D / Sexton PM / Miller LJ | |||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 33.4 KB 33.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.4 KB | Display | ![]() |
Images | ![]() | 108 KB | ||
Filedesc metadata | ![]() | 7.5 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() ![]() ![]() | 32 MB 59.6 MB 31.9 MB 59.5 MB 59.5 MB 59.5 MB 59.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 996.7 KB | Display | ![]() |
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Full document | ![]() | 996.3 KB | Display | |
Data in XML | ![]() | 16.4 KB | Display | |
Data in CIF | ![]() | 21.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9bkjMC ![]() 9bkkC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | best class, local refinement (micelle and ScFv16 masked out), sharpened | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: best class, local refinement (micelle, G protein, and...
File | emd_44642_additional_1.map | ||||||||||||
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Annotation | best class, local refinement (micelle, G protein, and ScFv16 masked out), unsharpened | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: best class, local refinement (micelle, G protein, and...
File | emd_44642_additional_2.map | ||||||||||||
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Annotation | best class, local refinement (micelle, G protein, and ScFv16 masked out), sharpened | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Consensus map, unsharpened
File | emd_44642_additional_3.map | ||||||||||||
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Annotation | Consensus map, unsharpened | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Consensus refinement, half map A
File | emd_44642_additional_4.map | ||||||||||||
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Annotation | Consensus refinement, half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Consensus refinement, half map B
File | emd_44642_additional_5.map | ||||||||||||
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Annotation | Consensus refinement, half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Best class, half-map B
File | emd_44642_half_map_1.map | ||||||||||||
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Annotation | Best class, half-map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Best class, half-map A
File | emd_44642_half_map_2.map | ||||||||||||
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Annotation | Best class, half-map A | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Complex of CCK1R (Y140A mutant) bound to miniGs (Gq, Gi chimera),...
Entire | Name: Complex of CCK1R (Y140A mutant) bound to miniGs (Gq, Gi chimera), G-beta1, G-gamma-2 and CCK8s. |
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Components |
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-Supramolecule #1: Complex of CCK1R (Y140A mutant) bound to miniGs (Gq, Gi chimera),...
Supramolecule | Name: Complex of CCK1R (Y140A mutant) bound to miniGs (Gq, Gi chimera), G-beta1, G-gamma-2 and CCK8s. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 Details: Single-chain fragment variable 16 (ScFv16) was included in the complex but left unmodeled. |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 150 KDa |
-Macromolecule #1: 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: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 37.413863 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: QSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC RFLDDNQIVT S SGDTTCAL ...String: QSELDQLRQE 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 |
-Macromolecule #2: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Macromolecule | Name: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 6.375332 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: NTASIAQARK LVEQLKMEAN IDRIKVSKAA ADLMAYCEAH AKEDPLLTPV PASENPFR UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 |
-Macromolecule #3: Cholecystokinin-8
Macromolecule | Name: Cholecystokinin-8 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.144255 KDa |
Sequence | String: D(TYS)MGWMDF UniProtKB: Cholecystokinin |
-Macromolecule #4: Cholecystokinin receptor type A
Macromolecule | Name: Cholecystokinin receptor type A / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 47.66277 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: DVVDSLLVNG SNITPPCELG LENETLFCLD QPRPSKEWQP AVQILLYSLI FLLSVLGNTL VITVLIRNKR MRTVTNIFLL SLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF MGTSVSVSTF NLVAISLERA GAICKPLQSR VWQTKSHALK V IAATWCLS ...String: DVVDSLLVNG SNITPPCELG LENETLFCLD QPRPSKEWQP AVQILLYSLI FLLSVLGNTL VITVLIRNKR MRTVTNIFLL SLAVSDLML CLFCMPFNLI PNLLKDFIFG SAVCKTTTYF MGTSVSVSTF NLVAISLERA GAICKPLQSR VWQTKSHALK V IAATWCLS FTIMTPYPIY SNLVPFTKNN NQTANMCRFL LPNDVMQQSW HTFLLLILFL IPGIVMMVAY GLISLELYQG IK FEASQKK SAKERKPSTT SSGKYEDSDG CYLQKTRPPR KLELRQLSTG SSSRANRIRS NSSAANLMAK KRVIRMLIVI VVL FFLCWM PIFSANAWRA YDTASAERRL SGTPISFILL LSYTSSCVNP IIYCFMNKRF RLGFMATFPC CPNPGPPGAR GEVG EEEEG GTTGASLSRF SYSHMSASVP PQ UniProtKB: Cholecystokinin receptor type A |
-Macromolecule #5: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine n...
Macromolecule | Name: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short type: protein_or_peptide / ID: 5 Details: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,with certain residues mutated to match Guanine nucleotide-binding protein G(q) subunit Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 29.144971 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: HHHHHHHHGC TLSAEDKAAV ERSKMIDRNL REDGEKARRT LRLLLLGADN SGKSTIVKQM RILHGGSGGS GGTSGIFETK FQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVDS SDYNRLQEAL NDFKSIWNNR WLRTISVILF LNKQDLLAEK V LAGKSKIE ...String: HHHHHHHHGC TLSAEDKAAV ERSKMIDRNL REDGEKARRT LRLLLLGADN SGKSTIVKQM RILHGGSGGS GGTSGIFETK FQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVDS SDYNRLQEAL NDFKSIWNNR WLRTISVILF LNKQDLLAEK V LAGKSKIE DYFPEFARYT TPEDATPEPG EDPRVTRAKY FIRKEFVDIS TASGDGRHIC YPHFTCAVDT ENARRIFNDC KD IILQMNL REYNLV UniProtKB: Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(s) subunit alpha isoforms short |
-Macromolecule #6: AMINO GROUP
Macromolecule | Name: AMINO GROUP / type: ligand / ID: 6 / Number of copies: 1 / Formula: NH2 |
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Molecular weight | Theoretical: 16.023 Da |
Chemical component information | ![]() ChemComp-NH2: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 5 mg/mL |
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Buffer | pH: 7.4 |
Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Details: 20 mA, negative polarity |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 5884 / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.6 µm |
Sample stage | Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |