[English] 日本語
![](img/lk-miru.gif)
- EMDB-40786: Structural basis and functional roles for Toll-like receptor bind... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structural basis and functional roles for Toll-like receptor binding to Latrophilin adhesion-GPCR in embryo development | |||||||||
![]() | Postprocessed map | |||||||||
![]() |
| |||||||||
![]() | synapse / C. elegans / ADGR / GPCR / CELL ADHESION | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.3 Å | |||||||||
![]() | Li J / Rosas GC / Arac D / Ozkan E | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Structural basis and functional roles for Toll-like receptor binding to Latrophilin adhesion-GPCR in embryo development Authors: Rosas GC / Li J / Smith J / Cheng S / Baltrusaitis E / Nawrocka W / Zhan M / Kratsios P / Arac D / Ozkan E | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 59.7 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 17.3 KB 17.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.2 KB | Display | ![]() |
Images | ![]() | 50.9 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 49.7 MB 49.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 823.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 823.2 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 21 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Postprocessed map | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.063 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: Halp map 1
File | emd_40786_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Halp map 1 | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Half map 2
File | emd_40786_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Half map 2 | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : The binary complex of C. elegans TOL-1 with C. elegans LAT-1 extr...
Entire | Name: The binary complex of C. elegans TOL-1 with C. elegans LAT-1 extracellular domains |
---|---|
Components |
|
-Supramolecule #1: The binary complex of C. elegans TOL-1 with C. elegans LAT-1 extr...
Supramolecule | Name: The binary complex of C. elegans TOL-1 with C. elegans LAT-1 extracellular domains type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: The Binary complex includes C.elegans Toll-like receptor 1 (Tol-1) and C. elegans Latrophilin 1 (LAT-1). |
---|---|
Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 172 KDa |
-Macromolecule #1: Toll-like receptor 1/TOL-1
Macromolecule | Name: Toll-like receptor 1/TOL-1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: ADPHHHHHHG SGLNDIFEAQ KIEWHEADPG YTDECPKFCK CAPDPVQPTS KLLLCDYSSK NTTITPIASS NYDQVANIRS LFISCDNNNF QFPDAYFKSL TALHHLRIVG CETTHFSVKL FEDLAALRRL ELDQISTAST SFEMTEDVLM PLARLEKFSL TRSRNIELPQ ...String: ADPHHHHHHG SGLNDIFEAQ KIEWHEADPG YTDECPKFCK CAPDPVQPTS KLLLCDYSSK NTTITPIASS NYDQVANIRS LFISCDNNNF QFPDAYFKSL TALHHLRIVG CETTHFSVKL FEDLAALRRL ELDQISTAST SFEMTEDVLM PLARLEKFSL TRSRNIELPQ RLLCSLPHLQ VLNISSNELP SLRREESCVA QQLLIVDLSR NRLTNIEQFL RGIPAIRQIS VAYNSIAELD LSLATPFLQQ LDAEANRIVD LTSLPGTVVH VNLAGNALKR VPDAVAELAS LVALNVSRNE IEAGNSSVFS SPELEMLDAS YNKLDSLPVE WLQKCEKRIA HLHLEHNSIE QLTGGVLANA TNLQTLDLSS NQLRVFRDEV LPENSKIGNL RLSNNSLELL EPSSLSGLKL ESLDLSHNKL TEVPAAIGKV EQLKKVDLSH NRIAKVYQYV LNKIKQLHTV DLSNNQLQSI GPYIFSDSSE LHSLDVSNNE ISLLFKDAFA RCPKLRKISM KMNKIKSLDE GLTEASGLRR LDVSHNEILV LKWSALPENL EILNADNNDI NLLTAASMSP STANLKSVSL SNNGITIMNA DQIPNSLESL DVSNNRLAKL GKTALAAKSQ LRRLNLKGNL LTVVATESMK VVEAVHPLKV EISENPLICD CQMGWMIGGA KPKVLIQDSE TASCSHAVDG HQIQIQSLSK KDLLCPYKSV CEPECICCQY GNCDCKSVCP ANCRCFRDDQ FNINIVRCHG NSSMVPKREF VVSELPVSAT EIILSGVTLP QLRTHSFIGR LRLQRLHING TGLRSIQPKA FHTLPALKTL DLSDNSLISL SGEEFLKCGE VSQLFLNGNR FSTLSRGIFE KLPNLKYLTL HNNSLEDIPQ VLHSTALSKI SLSSNPLRCD CSGGSQQHLH HRRDPKAHPF WEHNAAEWFS LHRHLVVDFP KVECWENVTK AFLTNDTTVL SAYPPNMGND VFVMPIEEFL RDYNSTICVP FSSGFFGQDP QNSDIQH |
-Macromolecule #2: Latrophilin 1/LAT-1
Macromolecule | Name: Latrophilin 1/LAT-1 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: AVPSNKPTTD ESGTISHTIC DGEAAELSCP AGKVISIVLG NYGRFSVAVC LPDNDIVPSN INCQNHKTKS ILEKKCNGDS MCYFTVDKKT FTEDPCPNTP KYLEVKYNCV VPATTTTTTT TTSTTTTDSS LIVDEEEEAQ KDALNSDVIK PVKKKEDVFC SATNRRGVNW ...String: AVPSNKPTTD ESGTISHTIC DGEAAELSCP AGKVISIVLG NYGRFSVAVC LPDNDIVPSN INCQNHKTKS ILEKKCNGDS MCYFTVDKKT FTEDPCPNTP KYLEVKYNCV VPATTTTTTT TTSTTTTDSS LIVDEEEEAQ KDALNSDVIK PVKKKEDVFC SATNRRGVNW QNTKSGTTSS APCPEGSSGK QLWACTEEGQ WLTEFPNSAG CESNWISSRN SVLSGVISSE DVSGLPEFLR NLGSETRRPM VGGDLPKVLH LLEKTVNVIA EESWAYQHLP LSNKGAVEVM NYMLRNQEIW GSWDVTKRKE FASRFILAAE KAMVASAKGM MTSAESNVIV QPAITVEISH KIKMSSQPTD YILFPSAALW NGQNVDNVNI PRDAILKINK DETQVFFSSF DNLGAQMTPS DVTVAIAGTD QTEVRKRRVV SRIVGASLIE NGKERRVENL TQPVRITFYH KESSVRHLSN PTCVWWNHHE LKWKPSGCKL SYHNKTMTSC DCTHLTHFAV LMDVRGHDLN EIDQTLLTHH HHHH |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 0.28 mg/mL |
---|---|
Buffer | pH: 8.5 / Details: 10 mM Tris, pH 8.5, 150 mM NaCl |
Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281.15 K / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number real images: 3333 / Average exposure time: 4.2 sec. / Average electron dose: 60.1 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |