› 1pfn

Solution NMR

PF4-M2 CHIMERIC MUTANT WITH THE FIRST 10 N-TERMINAL RESIDUES OF R-PF4 REPLACED BY THE N-TERMINAL RESIDUES OF THE IL8 SEQUENCE. MODELS 16-27 OF A 27-MODEL SET.

Released:
DOI: 10.2210/pdb1pfn/pdb
PDB entry 1pfn coloured by chain, ensemble of 12 models, front view.
PDB entry 1pfn coloured by chain, ensemble of 12 models, side view.
PDB entry 1pfn coloured by chain, ensemble of 12 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer.
Mayo KH, Roongta V, Ilyina E, Milius R, Barker S, Quinlan C, La Rosa G, Daly TJ
Biochemistry 34 11399-409 (1995)
PMID: 7547867

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-136202 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Platelet factor 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 68 amino acids
Theoretical weight: 7.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02776 (Residues: 38-101; Coverage: 91%)
Gene names: CXCL4, PF4, SCYB4
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
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Structure, function, and inhibition of chemokines.
Fernandez et al. (2002)
6 more

1 mention without citation

Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.
Del Poggetto et al. (2018)