› 2n54

Solution NMR

Solution structure of a disulfide stabilized XCL1 dimer

Released:
DOI: 10.2210/pdb2n54/pdb
PDB entry 2n54 coloured by chain, ensemble of 20 models, front view.
PDB entry 2n54 coloured by chain, ensemble of 20 models, side view.
PDB entry 2n54 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Engineering Metamorphic Chemokine Lymphotactin/XCL1 into the GAG-Binding, HIV-Inhibitory Dimer Conformation.
Fox JC, Tyler RC, Guzzo C, Tuinstra RL, Peterson FC, Lusso P, Volkman BF
ACS Chem Biol 10 2580-8 (2015)
PMID: 26302421

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lymphotactin Chains: A, B
Molecule details ›
Chains: A, B
Length: 93 amino acids
Theoretical weight: 10.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P47992 (Residues: 22-114; Coverage: 100%)
Gene names: LTN, SCYC1, XCL1
Sequence domains: Small cytokines (intecrine/chemokine), interleukin-8 like
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 81%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Mechanisms of Regulation of the Chemokine-Receptor Network.
Stone et al. (2017)
5 more

3 mentions without citation

Unfolding the Mysteries of Protein Metamorphosis.
Dishman et al. (2018)
2 more