› 4i80

X-ray diffraction
3.1Å resolution

Crystal structure of human menin in complex with a high-affinity macrocyclic peptidomimetics

Released:
DOI: 10.2210/pdb4i80/pdb
PDB entry 4i80 coloured by chain, front view.
PDB entry 4i80 coloured by chain, side view.
PDB entry 4i80 coloured by chain, top view.
Source organisms:
Primary publication:
Structure-based design of high-affinity macrocyclic peptidomimetics to block the menin-mixed lineage leukemia 1 (MLL1) protein-protein interaction.
Zhou H, Liu L, Huang J, Bernard D, Karatas H, Navarro A, Lei M, Wang S
J Med Chem 56 1113-23 (2013)
PMID: 23244744

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126205 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Menin Chain: A
Molecule details ›
Chain: A
Length: 550 amino acids
Theoretical weight: 61.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00255 (Residues: 2-610; Coverage: 90%)
Gene names: MEN1, SCG2
Sequence domains: Menin
macrocyclic peptidomimetic Chain: B
Molecule details ›
Chain: B
Length: 9 amino acids
Theoretical weight: 1.13 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P41212
Unit cell:
a: 141.379Å b: 141.379Å c: 92.879Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.245
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

16 review citations

Targeting protein-protein interactions as an anticancer strategy.
Ivanov et al. (2013)
15 more

4 mentions without citation

Challenges and opportunities in targeting the menin-MLL interaction.
Cierpicki et al. (2014)
3 more