8d74

Cryo-EM structure of human CNTF signaling complex: model containing the interaction core region

Method: ELECTRON MICROSCOPY Dmax: 165.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Interleukin-6 receptor subunit beta

Homo sapiens

UniProt P40189

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–619 Not recorded Ciliary neurotrophic factor × 1 (P26441) Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) Leukemia inhibitory factor receptor × 1 (P42702) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

19 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL6RB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–597; UniProt 23–619

Ciliary neurotrophic factor

Homo sapiens

UniProt P26441

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–186 Not recorded Interleukin-6 receptor subunit beta × 1 (P40189) Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) Leukemia inhibitory factor receptor × 1 (P42702) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNTF_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–186; UniProt 1–186

Ciliary neurotrophic factor receptor subunit alpha

Homo sapiens

UniProt P26992

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 23–342 Not recorded Interleukin-6 receptor subunit beta × 1 (P40189) Ciliary neurotrophic factor × 1 (P26441) Leukemia inhibitory factor receptor × 1 (P42702) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CNTFR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–320; UniProt 23–342

Leukemia inhibitory factor receptor

Homo sapiens

UniProt P42702

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 6 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 45–833 Not recorded Interleukin-6 receptor subunit beta × 1 (P40189) Ciliary neurotrophic factor × 1 (P26441) Ciliary neurotrophic factor receptor subunit alpha × 1 (P26992) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIFR_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–789; UniProt 45–833

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 8d74

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d74
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d74
Deposition date deposition_date2022-06-07
Structure title titleCryo-EM structure of human CNTF signaling complex: model containing the interaction core region
Keywords keywordscytokine signaling, CNTF, CNTFR alpha, gp130, LIFR, CYTOKINE; CYTOKINE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier48.69
Radius of gyration Rg (electron density) rg_electron49.09
Forward intensity I(0) i0270357000.00
Molecular weight molecular_weight136620.0 kDa
Excluded volume excluded_volume171730 ų
Envelope volume envelope_volume277990 ų
Hydration-shell volume shell_volume50895 ų
Envelope diameter envelope_diameter175.9
Shell Rg shell_rg48.35
Envelope Rg envelope_rg47.95
Shape Rg shape_rg49.08
Total Rg total_rg49.08
Total atoms total_atoms9639
Residues n_residues1163
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax165.5
Rg (real space) rg_real48.99
Rg uncertainty (real space) rg_real_error2.18
I(0) (real space) i0_real2.7040e+08
I(0) uncertainty (real space) i0_real_error5.6090e+06
Rg (reciprocal space) rg_reciprocal48.70
I(0) (reciprocal space) i0_reciprocal270300000.0000
Solution quality estimate total_estimate0.8560
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.7
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11270000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.606

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8d74A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8d74A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8d74D01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)