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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of human FcRL5 bound to IgG-Fc | |||||||||
Map data | Cryo-EM global map sharp of FcRL5 in complex with human IgG. | |||||||||
Sample |
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Keywords | IgG / FcRL5 / IMMUNE SYSTEM | |||||||||
| Function / homology | Function and homology informationB cell activation / immunoglobulin complex / single fertilization / coreceptor activity / transmembrane signaling receptor activity / adaptive immune response / cell surface receptor signaling pathway / receptor complex / immune response / external side of plasma membrane ...B cell activation / immunoglobulin complex / single fertilization / coreceptor activity / transmembrane signaling receptor activity / adaptive immune response / cell surface receptor signaling pathway / receptor complex / immune response / external side of plasma membrane / cell surface / extracellular region / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.56 Å | |||||||||
Authors | Chen SH / Xiao JY | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Sci Adv / Year: 2026Title: Human FcRL5 is an Fc receptor that simultaneously engages two IgGs. Authors: Shihua Chen / Shuhan Li / Zhiying Zhang / Junyu Xiao / ![]() Abstract: The Fc receptors play crucial roles in initiating the effector functions of immunoglobulins. FcRL5 is a prominent target in B cell malignancies and has been implicated as a receptor for ...The Fc receptors play crucial roles in initiating the effector functions of immunoglobulins. FcRL5 is a prominent target in B cell malignancies and has been implicated as a receptor for immunoglobulin G (IgG). However, the molecular mechanism remained unclear. Here, we demonstrate that human FcRL5, but not its mouse counterpart, is a bona fide IgG-Fc (Fcγ) receptor that uniquely requires the presence of two Fcγ molecules in close proximity to form a robust interaction. Cryo-electron microscopy reveals that FcRL5 optimally engages two Fcγ molecules positioned at a 60° angle, with its D1-D2 domains binding to the first Fcγ molecule, while its D3 domain arches over the second Fcγ. This distinctive binding capability enables FcRL5 to specifically recognize IgG immune complexes (ICs), with the binding strength correlating with IgG concentration in the ICs. In addition, we demonstrate that FcRL5 can internalize the IgG polymer and IC. These results shed light on FcRL5 function and reveal a unique Fcγ-FcγR binding mode governed by avidity. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_63244.map.gz | 197.8 MB | EMDB map data format | |
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| Header (meta data) | emd-63244-v30.xml emd-63244.xml | 21.6 KB 21.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_63244_fsc.xml | 12.5 KB | Display | FSC data file |
| Images | emd_63244.png | 20.8 KB | ||
| Filedesc metadata | emd-63244.cif.gz | 6.8 KB | ||
| Others | emd_63244_half_map_1.map.gz emd_63244_half_map_2.map.gz | 194.1 MB 194.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63244 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63244 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9locMC ![]() 9lodC M: atomic model generated by this map C: citing same article ( |
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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_63244.map.gz / Format: CCP4 / Size: 209.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM global map sharp of FcRL5 in complex with human IgG. | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| 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: Cryo-EM global map half A of FcRL5 in complex with human IgG.
| File | emd_63244_half_map_1.map | ||||||||||||
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| Annotation | Cryo-EM global map half A of FcRL5 in complex with human IgG. | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Cryo-EM global map half B of FcRL5 in complex with human IgG.
| File | emd_63244_half_map_2.map | ||||||||||||
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| Annotation | Cryo-EM global map half B of FcRL5 in complex with human IgG. | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Complex of human FcRL5 with IgG-Fc
| Entire | Name: Complex of human FcRL5 with IgG-Fc |
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| Components |
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-Supramolecule #1: Complex of human FcRL5 with IgG-Fc
| Supramolecule | Name: Complex of human FcRL5 with IgG-Fc / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Fc receptor-like protein 5
| Macromolecule | Name: Fc receptor-like protein 5 / 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: 94.512047 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: QFARTPRPII FLQPPWTTVF QGERVTLTCK GFRFYSPQKT KWYHRYLGKE ILRETPDNIL EVQESGEYRC QAQGSPLSSP VHLDFSSAS LILQAPLSVF EGDSVVLRCR AKAEVTLNNT IYKNDNVLAF LNKRTDFHIP HACLKDNGAY RCTGYKESCC P VSSNTVKI ...String: QFARTPRPII FLQPPWTTVF QGERVTLTCK GFRFYSPQKT KWYHRYLGKE ILRETPDNIL EVQESGEYRC QAQGSPLSSP VHLDFSSAS LILQAPLSVF EGDSVVLRCR AKAEVTLNNT IYKNDNVLAF LNKRTDFHIP HACLKDNGAY RCTGYKESCC P VSSNTVKI QVQEPFTRPV LRASSFQPIS GNPVTLTCET QLSLERSDVP LRFRFFRDDQ TLGLGWSLSP NFQITAMWSK DS GFYWCKA ATMPYSVISD SPRSWIQVQI PASHPVLTLS PEKALNFEGT KVTLHCETQE DSLRTLYRFY HEGVPLRHKS VRC ERGASI SFSLTTENSG NYYCTADNGL GAKPSKAVSL SVTVPVSHPV LNLSSPEDLI FEGAKVTLHC EAQRGSLPIL YQFH HEGAA LERRSANSAG GVAISFSLTA EHSGNYYCTA DNGFGPQRSK AVSLSVTVPV SHPVLTLSSA EALTFEGATV TLHCE VQRG SPQILYQFYH EDMPLWSSST PSVGRVSFSF SLTEGHSGNY YCTADNGFGP QRSEVVSLFV TVPVSRPILT LRVPRA QAV VGDLLELHCE APRGSPPILY WFYHEDVTLG SSSAPSGGEA SFNLSLTAEH SGNYSCEANN GLVAQHSDTI SLSVIVP VS RPILTFRAPR AQAVVGDLLE LHCEALRGSS PILYWFYHED VTLGKISAPS GGGASFNLSL TTEHSGIYSC EADNGLEA Q RSEMVTLKVA VPVSRPVLTL RAPGTHAAVG DLLELHCEAL RGSPLILYRF FHEDVTLGNR SSPSGGASLN LSLTAEHSG NYSCEADNGL GAQRSETVTL YITGLTANRS GPFATGHHHH HHHHWRPLES RVDYKDDDDK UniProtKB: Fc receptor-like protein 5 |
-Macromolecule #2: Immunoglobulin gamma-1 heavy chain
| Macromolecule | Name: Immunoglobulin gamma-1 heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 28.081764 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVS VLTVCHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP S DIAVEWES ...String: EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVS VLTVCHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP S DIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLDK STGKPTLYNV SL IMSDTGG TCY UniProtKB: Immunoglobulin gamma-1 heavy chain |
-Macromolecule #4: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 4 / Number of copies: 13 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.2 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TALOS ARCTICA |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 1.7 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
China, 1 items
Citation





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





































Processing
FIELD EMISSION GUN

