› 1tvx

X-ray diffraction
1.75Å resolution

NEUTROPHIL ACTIVATING PEPTIDE-2 VARIANT FORM M6L WITH FIVE ADDITIONAL AMINO TERMINAL RESIDUES (DSDLY)

Released:
DOI: 10.2210/pdb1tvx/pdb
PDB entry 1tvx coloured by chain, front view.
PDB entry 1tvx coloured by chain, side view.
PDB entry 1tvx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The amino-terminal residues in the crystal structure of connective tissue activating peptide-III (des10) block the ELR chemotactic sequence.
Malkowski MG, Lazar JB, Johnson PH, Edwards BF
J Mol Biol 266 367-80 (1997)
PMID: 9047370

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136198 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil-activating peptide 2(74) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 75 amino acids
Theoretical weight: 8.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02775 (Residues: 54-128; Coverage: 80%)
Gene names: CTAP3, CXCL7, PPBP, SCYB7, TGB1, THBGB1
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
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 43.81Å b: 76.76Å c: 43.78Å
α: 90° β: 96.95° γ: 90°
R-values:
R R work R free
0.196 0.196 0.251
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The role of CXC chemokines and their receptors in cancer.
Vandercappellen et al. (2008)
6 more

6 mentions without citation

The marriage of chemokines and galectins as functional heterodimers.
von Hundelshausen et al. (2021)
5 more