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Open data
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Basic information
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Title | Structure of the adhesion GPCR ADGRL3 in the apo state | |||||||||
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![]() | ADGRL3 / Apo form / ![]() | |||||||||
Function / homology | ![]() G protein-coupled receptor activity / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Tao Y / Guo Q / He B / Zhong Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: A method for structure determination of GPCRs in various states. Authors: Qiong Guo / Binbin He / Yixuan Zhong / Haizhan Jiao / Yinhang Ren / Qinggong Wang / Qiangqiang Ge / Yongxiang Gao / Xiangyu Liu / Yang Du / Hongli Hu / Yuyong Tao / ![]() Abstract: G-protein-coupled receptors (GPCRs) are a class of integral membrane proteins that detect environmental cues and trigger cellular responses. Deciphering the functional states of GPCRs induced by ...G-protein-coupled receptors (GPCRs) are a class of integral membrane proteins that detect environmental cues and trigger cellular responses. Deciphering the functional states of GPCRs induced by various ligands has been one of the primary goals in the field. Here we developed an effective universal method for GPCR cryo-electron microscopy structure determination without the need to prepare GPCR-signaling protein complexes. Using this method, we successfully solved the structures of the β-adrenergic receptor (βAR) bound to antagonistic and agonistic ligands and the adhesion GPCR ADGRL3 in the apo state. For βAR, an intermediate state stabilized by the partial agonist was captured. For ADGRL3, the structure revealed that inactive ADGRL3 adopts a compact fold and that large unusual conformational changes on both the extracellular and intracellular sides are required for activation of adhesion GPCRs. We anticipate that this method will open a new avenue for understanding GPCR structure‒function relationships and drug development. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.9 KB 13.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.4 KB | Display | ![]() |
Images | ![]() | 41.6 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 59.4 MB 59.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8jmtMC ![]() 8j7eC ![]() 8jj8C ![]() 8jjlC ![]() 8jjoC 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
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Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_36426_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_36426_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : ADGRL3-mBRIL complex
Entire | Name: ADGRL3-mBRIL complex |
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Components |
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-Supramolecule #1: ADGRL3-mBRIL complex
Supramolecule | Name: ADGRL3-mBRIL complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Adhesion G protein-coupled receptor L3,Soluble cytochrome b562
Macromolecule | Name: Adhesion G protein-coupled receptor L3,Soluble cytochrome b562 type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 86.362 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: DYKDDDDKAV EAREIMWFKT RQGQIAKQPC PAGTIGVSTY LCLAPDGIWD PQGPDLSNCS SPWVNHITQK LKSGETAANI ARELAEQTR NHLNAGDITY SVRAMDQLVG LLDVQLRNLT PGGKDSAARS LNKLQKRERS CRAYVQAMVE TVNNLLQPQA L NAWRDLTT ...String: DYKDDDDKAV EAREIMWFKT RQGQIAKQPC PAGTIGVSTY LCLAPDGIWD PQGPDLSNCS SPWVNHITQK LKSGETAANI ARELAEQTR NHLNAGDITY SVRAMDQLVG LLDVQLRNLT PGGKDSAARS LNKLQKRERS CRAYVQAMVE TVNNLLQPQA L NAWRDLTT SDQLRAATML LHTVEESAFV LADNLLKTDI VRENTDNIKL EVARLSTEGN LEDLKFPENM GHGSTIQLSA NT LKQNGRN GEIRVAFVLY NNLGPYLSTE NASMKLGTEA LSTNHSVIVN SPVITAAINK EFSNKVYLAD PVVFTVKHIK QSE ENFNPN CSFWSYSKRT MTGYWSTQGC RLLTTNKTHT TCSCNHLANF AVLMAHVEVK HSDAVHDLLL DVITWVGILL SLVC LLICI FTFCFFRGLQ SDRNTIHKNL CISLFVAELL FLIGINRTDQ PIACAVFAAL LHFFFLAAFT WMFLEGVQLY IMLVE VFES EHSRRKYFYL VGYGMPALIV AVSAAVDYRS YGTDKVCWLR LDTYFIWSFI GPATLIIMLN VIFLGIALYK MFHHTA DLE DNWETLNDNL KVIEKADNAA QVKDALTKMR AAALDAQKAT PPKLEDKSPD SPEMKDFRHG FDILVGQIDD ALKLANE GK VKEAQAAAEQ LKTTRNAYIQ KYLERADNIK SWVIGAIALL CLLGLTWAFG LMYINESTVI MAYLFTIFNS LQGMFIFI F HCVLQKKVRK EYGKCLRTHA ASRLEEELRR RLTEGSHHHH HHHH UniProtKB: Adhesion G protein-coupled receptor L3, Soluble cytochrome b562, Adhesion G protein-coupled receptor L3 |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |