› 2i9s

Solution NMR

The solution structure of the core of mesoderm development (MESD).

Released:
DOI: 10.2210/pdb2i9s/pdb
PDB entry 2i9s coloured by chain, ensemble of 20 models, front view.
PDB entry 2i9s coloured by chain, ensemble of 20 models, side view.
PDB entry 2i9s coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.
Köhler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H
J Struct Funct Genomics 7 131-8 (2006)
PMID: 17342452

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190175 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LRP chaperone MESD Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ERE7 (Residues: 89-184; Coverage: 49%)
Gene names: Mesd, Mesdc2
Sequence domains: Chaperone for wingless signalling and trafficking of LDL receptor
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Cooperative folding and ligand-binding properties of LRP6 beta-propeller domains.
Liu et al. (2009)
3 more

1 mention without citation

Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains.
Collins et al. (2011)