› 4nux

X-ray diffraction
2.3Å resolution

Structure of receptor A

Released:
DOI: 10.2210/pdb4nux/pdb
PDB entry 4nux coloured by chain, front view.
PDB entry 4nux coloured by chain, side view.
PDB entry 4nux coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling.
Zhang B, Liu C, Qian W, Han Y, Li X, Deng J
Acta Crystallogr D Biol Crystallogr 70 1476-83 (2014)
PMID: 24816115

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188488 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interleukin-17 receptor A Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 24.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96F46 (Residues: 376-591; Coverage: 26%)
Gene names: IL17R, IL17RA
Sequence domains: SEFIR domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 76.256Å b: 136.13Å c: 55.433Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.189 0.242
Expression system: Escherichia coli

Quick links

Citations

8 review citations

IL-17 Signaling: The Yin and the Yang.
Amatya et al. (2017)
7 more

3 mentions without citation

IL-17-receptor-associated adaptor Act1 directly stabilizes mRNAs to mediate IL-17 inflammatory signaling.
Herjan et al. (2018)
2 more