+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-41889 | |||||||||
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Title | Structure of CXCL12-bound CXCR4/Gi complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | GPCR / chemokine receptor / chemokine / SIGNALING PROTEIN | |||||||||
Function / homology | Function and homology information C-X-C motif chemokine 12 receptor activity / regulation of viral process / chemokine (C-X-C motif) ligand 12 signaling pathway / negative regulation of leukocyte tethering or rolling / positive regulation of vascular wound healing / positive regulation of macrophage migration inhibitory factor signaling pathway / positive regulation of mesenchymal stem cell migration / neuron recognition / response to ultrasound / response to tacrolimus ...C-X-C motif chemokine 12 receptor activity / regulation of viral process / chemokine (C-X-C motif) ligand 12 signaling pathway / negative regulation of leukocyte tethering or rolling / positive regulation of vascular wound healing / positive regulation of macrophage migration inhibitory factor signaling pathway / positive regulation of mesenchymal stem cell migration / neuron recognition / response to ultrasound / response to tacrolimus / telencephalon cell migration / regulation of actin polymerization or depolymerization / C-X-C chemokine receptor activity / Specification of primordial germ cells / CXCL12-activated CXCR4 signaling pathway / chemokine receptor binding / myosin light chain binding / myelin maintenance / positive regulation of vasculature development / regulation of programmed cell death / CXCR chemokine receptor binding / positive regulation of axon extension involved in axon guidance / C-C chemokine receptor activity / endothelial tube morphogenesis / positive regulation of dopamine secretion / endothelial cell differentiation / C-C chemokine binding / Signaling by ROBO receptors / regulation of chemotaxis / cellular response to organonitrogen compound / positive regulation of chemotaxis / Formation of definitive endoderm / induction of positive chemotaxis / integrin activation / positive regulation of dendrite extension / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / negative regulation of dendritic cell apoptotic process / cellular response to chemokine / chemokine-mediated signaling pathway / anchoring junction / blood circulation / positive regulation of monocyte chemotaxis / Chemokine receptors bind chemokines / chemokine activity / dendritic cell chemotaxis / positive regulation of oligodendrocyte differentiation / epithelial cell development / positive regulation of calcium ion import / cell leading edge / cellular response to cytokine stimulus / detection of temperature stimulus involved in sensory perception of pain / regulation of calcium ion transport / positive regulation of cell adhesion / Adenylate cyclase inhibitory pathway / positive regulation of protein localization to cell cortex / positive regulation of T cell migration / regulation of cAMP-mediated signaling / Binding and entry of HIV virion / small molecule binding / animal organ regeneration / D2 dopamine receptor binding / G protein-coupled serotonin receptor binding / regulation of cell adhesion / coreceptor activity / detection of mechanical stimulus involved in sensory perception of pain / Nuclear signaling by ERBB4 / regulation of mitotic spindle organization / cellular response to forskolin / cardiac muscle contraction / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / positive regulation of endothelial cell proliferation / positive regulation of neuron differentiation / cell chemotaxis / neurogenesis / adult locomotory behavior / response to activity / ubiquitin binding / Regulation of insulin secretion / G protein-coupled receptor activity / G protein-coupled receptor binding / calcium-mediated signaling / axon guidance / neuron migration / growth factor activity / Olfactory Signaling Pathway / G-protein beta/gamma-subunit complex binding / brain development / response to virus / Activation of the phototransduction cascade / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / 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 / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.29 Å | |||||||||
Authors | Saotome K / McGoldrick LL / Franklin MC | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Biorxiv / Year: 2024 Title: Structural insights into CXCR4 modulation and oligomerization Authors: Saotome K / McGoldrick LL / Ho J / Ramlall T / Shah S / Moore MJ / Kim JH / Leidich R / Olson WC / Franklin MC | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_41889.map.gz | 97.2 MB | EMDB map data format | |
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Header (meta data) | emd-41889-v30.xml emd-41889.xml | 19.8 KB 19.8 KB | Display Display | EMDB header |
Images | emd_41889.png | 99.7 KB | ||
Filedesc metadata | emd-41889.cif.gz | 6.4 KB | ||
Others | emd_41889_half_map_1.map.gz emd_41889_half_map_2.map.gz | 95.6 MB 95.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-41889 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-41889 | HTTPS FTP |
-Related structure data
Related structure data | 8u4oMC 8u4nC 8u4pC 8u4qC 8u4rC 8u4sC 8u4tC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_41889.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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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
-Half map: #1
File | emd_41889_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_41889_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : CXCL12-bound CXCR4/Gi complex
Entire | Name: CXCL12-bound CXCR4/Gi complex |
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Components |
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-Supramolecule #1: CXCL12-bound CXCR4/Gi complex
Supramolecule | Name: CXCL12-bound CXCR4/Gi complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: C-X-C chemokine receptor type 4
Macromolecule | Name: C-X-C chemokine receptor type 4 / 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: 71.063609 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MKTIIALSYI FCLVFAGAPE GISIYTSDNY TEEMGSGDYD SMKEPCFREE NANFNKIFLP TIYSIIFLTG IVGNGLVILV MGYQKKLRS MTDKYRLHLS VADLLFVITL PFWAVDAVAN WYFGNFLCKA VHVIYTVSLY SSVLILAFIS LDRYLAIVHA T NSQRPRKL ...String: MKTIIALSYI FCLVFAGAPE GISIYTSDNY TEEMGSGDYD SMKEPCFREE NANFNKIFLP TIYSIIFLTG IVGNGLVILV MGYQKKLRS MTDKYRLHLS VADLLFVITL PFWAVDAVAN WYFGNFLCKA VHVIYTVSLY SSVLILAFIS LDRYLAIVHA T NSQRPRKL LAEKVVYVGV WIPALLLTIP DFIFANVSEA DDRYICDRFY PNDLWVVVFQ FQHIMVGLIL PGIVILSCYC II ISKLSHS KGHQKRKALK TTVILILAFF ACWLPYYIGI SIDSFILLEI IKQGCEFENT VHKWISITEA LAFFHCCLNP ILY AFLGAK FKTSAQHALT SVSRGSSLKI LSKGKRGGHS SVSTESESSS FHSSGRPLEV LFQGPGGGGS VSKGEELFTG VVPI LVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQ ERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI DFKEDGNILG HKLEYNYNSH NVYIMADKQK NGIKVNFKIR HNIEDG SVQ LADHYQQNTP IGDGPVLLPD NHYLSTQSKL SKDPNEKRDH MVLLEFVTAA GITLGMDELY KDYKDDDDK UniProtKB: C-X-C chemokine receptor type 4 |
-Macromolecule #2: Guanine nucleotide-binding protein G(i) subunit alpha-1
Macromolecule | Name: Guanine nucleotide-binding protein G(i) subunit alpha-1 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: 41.591312 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MHHHHHHGGG GSGCTLSAED KAAVERSKMI DRNLREDGEK AAREVKLLLL GAGESGKCTI VKQMKIIHEA GYSEEECKQY KAVVYSNTI QSIIAIIRAM GRLKIDFGDS ARADDARQLF VLAGAAEEGF MTAELAGVIK RLWKDSGVQA CFNRSREYQL N DSAAYYLN ...String: MHHHHHHGGG GSGCTLSAED KAAVERSKMI DRNLREDGEK AAREVKLLLL GAGESGKCTI VKQMKIIHEA GYSEEECKQY KAVVYSNTI QSIIAIIRAM GRLKIDFGDS ARADDARQLF VLAGAAEEGF MTAELAGVIK RLWKDSGVQA CFNRSREYQL N DSAAYYLN DLDRIAQPNY IPTQQDVLRT RVKTTGIVET HFTFKDLHFK MFDVTAQRSE RKKWIHCFEG VTAIIFCVAL SD YDLVLAE DEEMNRMHAS MKLFDSICNN KWFTDTSIIL FLNKKDLFEE KIKKSPLTIC YPEYAGSNTY EEAAAYIQCQ FED LNKRKD TKEIYTHFTC STDTKNVQFV FDAVTDVIIK NNLKDCGLF UniProtKB: Guanine nucleotide-binding protein G(i) subunit alpha-1 |
-Macromolecule #3: 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: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 38.534062 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MHHHHHHGSS GSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKL IIWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC R FLDDNQIV ...String: MHHHHHHGSS GSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKL IIWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC R FLDDNQIV TSSGDTTCAL WDIETGQQTT TFTGHTGDVM SLSLAPDTRL FVSGACDASA KLWDVREGMC RQTFTGHESD IN AICFFPN GNAFATGSDD ATCRLFDLRA DQELMTYSHD NIICGITSVS FSKSGRLLLA GYDDFNCNVW DALKADRAGV LAG HDNRVS CLGVTDDGMA VATGSWDSFL KIWN UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 |
-Macromolecule #4: 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: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 7.861143 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFCAI L UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 |
-Macromolecule #5: Stromal cell-derived factor 1
Macromolecule | Name: Stromal cell-derived factor 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: 7.97846 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK UniProtKB: Stromal cell-derived factor 1 |
-Macromolecule #6: CHOLESTEROL
Macromolecule | Name: CHOLESTEROL / type: ligand / ID: 6 / Number of copies: 1 / Formula: CLR |
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Molecular weight | Theoretical: 386.654 Da |
Chemical component information | ChemComp-CLR: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.29 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 87963 |