› 1mv3

Solution NMR

NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC

Released:
DOI: 10.2210/pdb1mv3/pdb
PDB entry 1mv3 coloured by chain, ensemble of 20 models, front view.
PDB entry 1mv3 coloured by chain, ensemble of 20 models, side view.
PDB entry 1mv3 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants.
Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, Muhandiram R, Lu Y, Seet BT, Katz S, Szyperski T, Penn LZ, Arrowsmith CH
J Mol Biol 351 182-94 (2005)
PMID: 15992821

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myc box-dependent-interacting protein 1 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 22.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00499 (Residues: 301-593; Coverage: 36%)
Gene names: AMPHL, BIN1
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

33 review citations

Function of alternative splicing.
Kelemen et al. (2013)
32 more

2 mentions without citation

The sarcomeric M-region: a molecular command center for diverse cellular processes.
Hu et al. (2015)
1 more