› 5ixd

X-ray diffraction
2.85Å resolution

Structure of human JAK1 FERM/SH2 in complex with IFN lambda receptor

Released:
DOI: 10.2210/pdb5ixd/pdb
PDB entry 5ixd coloured by chain, front view.
PDB entry 5ixd coloured by chain, side view.
PDB entry 5ixd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Structural Basis for Class II Cytokine Receptor Recognition by JAK1.
Ferrao R, Wallweber HJ, Ho H, Tam C, Franke Y, Quinn J, Lupardus PJ
Structure 24 897-905 (2016)
PMID: 27133025

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149970 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase JAK1 Chain: A
Molecule details ›
Chain: A
Length: 544 amino acids
Theoretical weight: 63.36 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P23458 (Residues: 35-559; Coverage: 46%)
Gene names: JAK1, JAK1A, JAK1B
Sequence domains:
Interferon lambda receptor 1 Chain: B
Molecule details ›
Chain: B
Length: 55 amino acids
Theoretical weight: 6.14 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8IU57 (Residues: 250-299; Coverage: 10%)
Gene names: IFNLR1, IL28RA, LICR2

Ligands and Environments

1 bound ligand:
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: C2221
Unit cell:
a: 111.17Å b: 193.2Å c: 72.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.249 0.282
Expression system: Spodoptera frugiperda

Quick links

Citations

11 review citations

Mechanisms and consequences of Jak-STAT signaling in the immune system.
Villarino et al. (2017)
10 more

7 mentions without citation

The Janus Kinase (JAK) FERM and SH2 Domains: Bringing Specificity to JAK-Receptor Interactions.
Ferrao et al. (2017)
6 more