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Yorodumi- EMDB-33984: Complex structure of Neuropeptide Y Y2 receptor in complex with P... -
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Basic information
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| Title | Complex structure of Neuropeptide Y Y2 receptor in complex with PYY(3-36) and Gi | |||||||||
Map data | Composite map | |||||||||
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| Function / homology | Function and homology informationregulation of peptide secretion / negative regulation of neuronal action potential / peptide YY receptor activity / negative regulation of peptide secretion / neuropeptide Y receptor activity / negative regulation of eating behavior / neuropeptide Y receptor binding / intestinal epithelial cell differentiation / cardiac left ventricle morphogenesis / neuropeptide receptor activity ...regulation of peptide secretion / negative regulation of neuronal action potential / peptide YY receptor activity / negative regulation of peptide secretion / neuropeptide Y receptor activity / negative regulation of eating behavior / neuropeptide Y receptor binding / intestinal epithelial cell differentiation / cardiac left ventricle morphogenesis / neuropeptide receptor activity / 9+0 non-motile cilium / neuropeptide hormone activity / feeding behavior / outflow tract morphogenesis / G-protein alpha-subunit binding / regulation of eating behavior / adenylate cyclase inhibitor activity / T cell migration / positive regulation of protein localization to cell cortex / positive regulation of relaxation of smooth muscle / Adenylate cyclase inhibitory pathway / D2 dopamine receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / G protein-coupled serotonin receptor binding / locomotory behavior / cellular response to forskolin / regulation of mitotic spindle organization / Peptide ligand-binding receptors / mast cell degranulation / chemokine-mediated signaling pathway / calcium channel regulator activity / neuropeptide signaling pathway / Regulation of insulin secretion / response to prostaglandin E / hormone activity / positive regulation of cholesterol biosynthetic process / G protein-coupled receptor binding / response to peptide hormone / G-protein beta/gamma-subunit complex binding / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / Olfactory Signaling Pathway / Activation of the phototransduction cascade / G protein-coupled acetylcholine receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / cilium / Prostacyclin signalling through prostacyclin receptor / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / GDP binding / photoreceptor disc membrane / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / 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 / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / ADORA2B mediated anti-inflammatory cytokines production / adenylate cyclase-activating dopamine receptor signaling pathway / cellular response to prostaglandin E stimulus / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / heterotrimeric G-protein complex / Inactivation, recovery and regulation of the phototransduction cascade / G alpha (12/13) signalling events / G-protein beta-subunit binding / extracellular vesicle / Thrombin signalling through proteinase activated receptors (PARs) / adenylate cyclase-activating G protein-coupled receptor signaling pathway / signaling receptor complex adaptor activity / signaling receptor activity / ciliary basal body / GTPase binding / midbody / G protein activity / Ca2+ pathway / cell cortex / 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 / G alpha (q) signalling events / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Ras protein signal transduction / Extra-nuclear estrogen signaling / G protein-coupled receptor signaling pathway / receptor ligand activity / cell division / lysosomal membrane / centrosome Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) / ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | |||||||||
Authors | Kang H / Park C / Kim J / Choi H-J | |||||||||
| Funding support | Korea, Republic Of, 2 items
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Citation | Journal: Structure / Year: 2023Title: Structural basis for Y2 receptor-mediated neuropeptide Y and peptide YY signaling. Authors: Hyunook Kang / Chaehee Park / Yeol Kyo Choi / Jungnam Bae / Sohee Kwon / Jinuk Kim / Chulwon Choi / Chaok Seok / Wonpil Im / Hee-Jung Choi / ![]() Abstract: Neuropeptide Y (NPY) and its receptors are expressed in various human tissues including the brain where they regulate appetite and emotion. Upon NPY stimulation, the neuropeptide Y1 and Y2 receptors ...Neuropeptide Y (NPY) and its receptors are expressed in various human tissues including the brain where they regulate appetite and emotion. Upon NPY stimulation, the neuropeptide Y1 and Y2 receptors (YR and YR, respectively) activate G signaling, but their physiological responses to food intake are different. In addition, deletion of the two N-terminal amino acids of peptide YY (PYY(3-36)), the endogenous form found in circulation, can stimulate YR but not YR, suggesting that YR and YR may have distinct ligand-binding modes. Here, we report the cryo-electron microscopy structures of the PYY(3-36)‒YR‒G and NPY‒YR‒G complexes. Using cell-based assays, molecular dynamics simulations, and structural analysis, we revealed the molecular basis of the exclusive binding of PYY(3-36) to YR. Furthermore, we demonstrated that YR favors G protein signaling over β-arrestin signaling upon activation, whereas YR does not show a preference between these two pathways. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_33984.map.gz | 228.8 MB | EMDB map data format | |
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| Header (meta data) | emd-33984-v30.xml emd-33984.xml | 26.1 KB 26.1 KB | Display Display | EMDB header |
| Images | emd_33984.png | 88.1 KB | ||
| Others | emd_33984_additional_1.map.gz emd_33984_additional_2.map.gz | 230 MB 230.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33984 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33984 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7yonMC ![]() 7yooC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_33984.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Composite map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.849 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Local refined map of G-protein complex
| File | emd_33984_additional_1.map | ||||||||||||
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| Annotation | Local refined map of G-protein complex | ||||||||||||
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| Density Histograms |
-Additional map: Local refined map of PYY(3-36)-Y2R
| File | emd_33984_additional_2.map | ||||||||||||
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| Annotation | Local refined map of PYY(3-36)-Y2R | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Complex structure of PYY(3-36)-Y2R-Gi-scFv16
+Supramolecule #1: Complex structure of PYY(3-36)-Y2R-Gi-scFv16
+Supramolecule #2: Guanine nucleotide-binding protein
+Supramolecule #3: scFv16
+Supramolecule #4: PYY(3-36)
+Macromolecule #1: Guanine nucleotide-binding protein G(i) subunit alpha-1
+Macromolecule #2: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
+Macromolecule #3: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
+Macromolecule #4: Peptide YY(3-36)
+Macromolecule #5: Neuropeptide Y receptor type 2
+Macromolecule #6: single-chain antibody Fv fragment (scFv16)
+Macromolecule #7: water
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 10 mg/mL |
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| Buffer | pH: 7.5 |
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.5 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.75 µm |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Homo sapiens (human)
Authors
Korea, Republic Of, 2 items
Citation







































Z (Sec.)
Y (Row.)
X (Col.)




































Trichoplusia ni (cabbage looper)
Processing
FIELD EMISSION GUN


