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Open data
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Basic information
| Entry | Database: PDB / ID: 9lod | ||||||||||||||||||||||||||||||
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| Title | Local structure of human FcRL5 bound to IgG-Fc | ||||||||||||||||||||||||||||||
Components |
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Keywords | IMMUNE SYSTEM / IgG / FcRL5 | ||||||||||||||||||||||||||||||
| 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 | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.16 Å | ||||||||||||||||||||||||||||||
Authors | Chen, S.H. / Xiao, J.Y. | ||||||||||||||||||||||||||||||
| Funding support | China, 1items
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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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9lod.cif.gz | 248.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9lod.ent.gz | 190.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9lod.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lo/9lod ftp://data.pdbj.org/pub/pdb/validation_reports/lo/9lod | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 63245MC ![]() 9locC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 94512.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FCRL5, FCRH5, IRTA2, UNQ503/PRO820 / Production host: Homo sapiens (human) / References: UniProt: Q96RD9 | ||||||||||
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| #2: Antibody | Mass: 28081.764 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) / References: UniProt: P0DOX5#3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | #4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | #5: Sugar | ChemComp-NAG / | Has ligand of interest | Y | Has protein modification | Y | |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Complex of human FcRL5 with IgG-Fc / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.2 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: OTHER / Nominal defocus max: 1700 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.16 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 257893 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
China, 1items
Citation


PDBj






FIELD EMISSION GUN