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8wkw

Structure of MAVS-CARD Filament

Method: ELECTRON MICROSCOPY Dmax: 161.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Mitochondrial antiviral-signaling protein

Homo sapiens

UniProt Q7Z434

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 26 PDB declaration: 26-meric（26） Consistent with protein copy count Chain A； UniProt 1–97 Chain B； UniProt 1–97 Chain C； UniProt 1–97 Chain D； UniProt 1–97 Chain E； UniProt 1–97 Chain F； UniProt 1–97 Chain G； UniProt 1–97 Chain H； UniProt 1–97 Chain I； UniProt 1–97 Chain J； UniProt 1–97 Chain K； UniProt 1–97 Chain L； UniProt 1–97 Chain M； UniProt 1–97 Chain N； UniProt 1–97 Chain O； UniProt 1–97 Chain P； UniProt 1–97 Chain Q； UniProt 1–97 Chain R； UniProt 1–97 Chain S； UniProt 1–97 Chain T； UniProt 1–97 Chain U； UniProt 1–97 Chain V； UniProt 1–97 Chain W； UniProt 1–97 Chain X； UniProt 1–97 Chain Y； UniProt 1–97 Chain Z； UniProt 1–97 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.21 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8WKW Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2MS7 High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD Deposited 2014-07-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 21 PDB declaration: 21-meric
Chain A 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain B 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain C 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain D 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain E 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain F 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain G 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain H 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain I 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain J 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain K 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain L 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain M 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain N 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain O 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain P 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain Q 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain R 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain S 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain T 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Chain U 1–100（100 aa） Fragment：UNP RESIDUES 1-100
Not recorded No recorded non-water small molecule SOLID-STATE NMR
NMR measurement conditions pH 7；278 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 20 mM [U-99% 13C; U-99% 15N] MAVS CARD-1, H2O | H2O
NMR sample composition 20 mM [1-13C]-Glc U-15N MAVS CARD-2, H2O | H2O
NMR sample composition 20 mM [2-13C]-Glc U-15N MAVS CARD-3, H2O | H2O
NMR sample composition 20 mM [1/2-13C]-Glc(mixed) U15N MAVS CARD-4, H2O | H2O
NMR sample composition 20 mM [U-99% 13C; U-99% 15N] 1:6(Unlabeled) Diluted sample MAVS CARD-5, H2O | H2O
NMR sample composition 20 mM U15N mixed with U13C labeled sample MAVS CARD-6, H2O | H2O
Resolution not provided
2MS8 Solution NMR structure of MAVS CARD Deposited 2014-07-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–100（100 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient
NMR sample composition 300 uM [U-99% 13C; U-99% 15N] MAVS CARD-1, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
2VGQ Crystal Structure of Human IPS-1 CARD Deposited 2007-11-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–93（93 aa） Fragment：MMBP RESIDUES 27-392, CARD DOMAIN RESIDUES 3-93,MMBP RESIDUES 27-392, CARD DOMAIN RESIDUES 3-93
Not recorded SO4 SULFATE ION × 5 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.10 Å R-free 0.220
3J6C Cryo-EM structure of MAVS CARD filament Deposited 2014-02-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 3–93（91 aa） Fragment：caspase activation recruitment domain (UNP residues 3-93)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT；pH 7.5；20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT
cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane (FEI VITROBOT MARK III)
Resolution 9.60 Å
3J6C Cryo-EM structure of MAVS CARD filament Deposited 2014-02-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–93（91 aa） Fragment：caspase activation recruitment domain (UNP residues 3-93)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT；pH 7.5；20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT
cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane (FEI VITROBOT MARK III)
Resolution 9.60 Å
3J6C Cryo-EM structure of MAVS CARD filament Deposited 2014-02-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–93（91 aa） Fragment：caspase activation recruitment domain (UNP residues 3-93)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT；pH 7.5；20 mM Tris-HCl, 50 mM NaCl, 1 mM DTT
cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane (FEI VITROBOT MARK III)
Resolution 9.60 Å
3J6J 3.6 Angstrom resolution MAVS filament generated from helical reconstruction Deposited 2014-03-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain B 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain C 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain D 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain E 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain G 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain I 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Chain L 1–97（97 aa） Fragment：N-terminal CARD domain (UNP residues 1-97)
Mutation：P2A Mutation：P2A Mutation：P2A Mutation：P2A Mutation：P2A Mutation：P2A Mutation：P2A Mutation：P2A No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 mM Tris, 150 mM NaCl；pH 7.5；20 mM Tris, 150 mM NaCl
cryo-EM vitrification conditions Cryogen NITROGEN；Plunged in liquid nitrogen (FEI VITROBOT MARK I)
Resolution 3.64 Å R-free 0.276
4P4H Caught-in-action signaling complex of RIG-I 2CARD domain and MAVS CARD domain Deposited 2014-03-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 21 PDB declaration: 21-meric
Chain I 1–99（99 aa）
Chain J 1–99（99 aa）
Chain K 1–99（99 aa）
Chain L 1–99（99 aa）
Chain M 1–99（99 aa）
Chain N 1–99（99 aa）
Chain O 1–99（99 aa）
Chain P 1–99（99 aa）
Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；Tri-Li Citrate, PEG 3350, Cr(III) Cl3
Resolution 3.40 Å R-free 0.240
4Z8M Crystal structure of the MAVS-TRAF6 complex Deposited 2015-04-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 450–468（19 aa） Fragment：UNP residues 450-468
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；6% (v/v) Tacsimate pH 6.0, 0.1 M MES pH 6.0, and 25% (w/v) polyethylene glycol 4000
Resolution 2.95 Å R-free 0.238
4Z8M Crystal structure of the MAVS-TRAF6 complex Deposited 2015-04-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 450–468（19 aa） Fragment：UNP residues 450-468
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；6% (v/v) Tacsimate pH 6.0, 0.1 M MES pH 6.0, and 25% (w/v) polyethylene glycol 4000
Resolution 2.95 Å R-free 0.238
7DNI MDA5 CARDs-MAVS CARD polyUb complex Deposited 2020-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain M 1–97（97 aa）
Chain N 1–97（97 aa）
Chain O 1–97（97 aa）
Chain P 1–97（97 aa）
Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K Mutation：D23K, E26K, E80K No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
Resolution 3.20 Å

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAVS_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–97； UniProt 1–97 Author chain B； PDBConstruct 1–97； UniProt 1–97 Author chain C； PDBConstruct 1–97； UniProt 1–97 Author chain D； PDBConstruct 1–97； UniProt 1–97 Author chain E； PDBConstruct 1–97； UniProt 1–97 Author chain F； PDBConstruct 1–97； UniProt 1–97 Author chain G； PDBConstruct 1–97； UniProt 1–97 Author chain H； PDBConstruct 1–97； UniProt 1–97 Author chain I； PDBConstruct 1–97； UniProt 1–97 Author chain J； PDBConstruct 1–97； UniProt 1–97 Author chain K； PDBConstruct 1–97； UniProt 1–97 Author chain L； PDBConstruct 1–97； UniProt 1–97 Author chain M； PDBConstruct 1–97； UniProt 1–97 Author chain N； PDBConstruct 1–97； UniProt 1–97 Author chain O； PDBConstruct 1–97； UniProt 1–97 Author chain P； PDBConstruct 1–97； UniProt 1–97 Author chain Q； PDBConstruct 1–97； UniProt 1–97 Author chain R； PDBConstruct 1–97； UniProt 1–97 Author chain S； PDBConstruct 1–97； UniProt 1–97 Author chain T； PDBConstruct 1–97； UniProt 1–97 Author chain U； PDBConstruct 1–97； UniProt 1–97 Author chain V； PDBConstruct 1–97； UniProt 1–97 Author chain W； PDBConstruct 1–97； UniProt 1–97 Author chain X； PDBConstruct 1–97； UniProt 1–97 Author chain Y； PDBConstruct 1–97； UniProt 1–97 Author chain Z； PDBConstruct 1–97； UniProt 1–97

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8wkw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wkw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wkw
Deposition date deposition_date2023-09-28
Structure title titleStructure of MAVS-CARD Filament
Keywords keywordsFilament, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier46.94 Å
Radius of gyration Rg (electron density) rg_electron47.11 Å
Forward intensity I(0) i01266500000.00
Molecular weight molecular_weight293750.0 kDa
Excluded volume excluded_volume366600 ų
Envelope volume envelope_volume509330 ų
Hydration-shell volume shell_volume90019 ų
Envelope diameter envelope_diameter168.3 Å
Shell Rg shell_rg50.97 Å
Envelope Rg envelope_rg46.75 Å
Shape Rg shape_rg47.14 Å
Total Rg total_rg47.18 Å
Total atoms total_atoms20670
Residues n_residues2522
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax161.8 Å
Rg (real space) rg_real47.15 Å
Rg uncertainty (real space) rg_real_error1.45 Å
I(0) (real space) i0_real1.2660e+09
I(0) uncertainty (real space) i0_real_error2.3490e+07
Rg (reciprocal space) rg_reciprocal46.94 Å
I(0) (reciprocal space) i0_reciprocal1266000000.0000
Solution quality estimate total_estimate0.8382
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.6 Å
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha879700000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.705; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.777
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)