› 4cgc

X-ray diffraction
2.9Å resolution

Crystal structure of the trimerization domain of human EML4

Released:
DOI: 10.2210/pdb4cgc/pdb
PDB entry 4cgc coloured by chain, front view.
PDB entry 4cgc coloured by chain, side view.
PDB entry 4cgc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein require an N-terminal trimerization domain.
Richards MW, O'Regan L, Roth D, Montgomery JM, Straube A, Fry AM, Bayliss R
Biochem J 467 529-36 (2015)
PMID: 25740311

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Echinoderm microtubule-associated protein-like 4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 59 amino acids
Theoretical weight: 6.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HC35 (Residues: 6-64; Coverage: 6%)
Gene names: C2orf2, EMAPL4, EML4

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P43212
Unit cell:
a: 67.491Å b: 67.491Å c: 50.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.268 0.292
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

EML4-ALK Variants: Biological and Molecular Properties, and the Implications for Patients.
Sabir et al. (2017)
12 more

4 mentions without citation

Molecular mechanisms that underpin EML4-ALK driven cancers and their response to targeted drugs.
Bayliss et al. (2016)
3 more