› 2a93

Solution NMR

NMR SOLUTION STRUCTURE OF THE C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER, 40 STRUCTURES

Released:
DOI: 10.2210/pdb2a93/pdb
PDB entry 2a93 coloured by chain, ensemble of 40 models, front view.
PDB entry 2a93 coloured by chain, ensemble of 40 models, side view.
PDB entry 2a93 coloured by chain, ensemble of 40 models, top view.
Source organisms:
Primary publication:
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
J Mol Biol 281 165-81 (1998)
PMID: 9680483

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133946 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Myc proto-oncogene protein Chain: A
Molecule details ›
Chain: A
Length: 34 amino acids
Theoretical weight: 3.84 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01106 (Residues: 420-449; Coverage: 7%)
Gene names: BHLHE39, MYC
Sequence domains: Myc leucine zipper domain
Protein max Chain: B
Molecule details ›
Chain: B
Length: 34 amino acids
Theoretical weight: 3.78 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P28574 (Residues: 74-102; Coverage: 18%)
Gene names: Max, Myn

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

7 review citations

Coiled coils: a highly versatile protein folding motif.
Burkhard et al. (2001)
6 more

5 mentions without citation

Homodimeric and Heterodimeric Interactions among Vertebrate Basic Helix-Loop-Helix Transcription Factors.
Torres-Machorro AL. (2021)
4 more