› 2l64

Solution NMR

NMR Solution structure of GLP-2 in DHPC micelles

Released:
DOI: 10.2210/pdb2l64/pdb
PDB entry 2l64 coloured by chain, ensemble of 10 models, front view.
PDB entry 2l64 coloured by chain, ensemble of 10 models, side view.
PDB entry 2l64 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain.
Venneti KC, Hewage CM
FEBS Lett 585 346-52 (2011)
PMID: 21167157

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134154 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucagon-like peptide 2 Chain: A
Molecule details ›
Chain: A
Length: 33 amino acids
Theoretical weight: 3.77 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01275 (Residues: 146-178; Coverage: 21%)
Gene name: GCG
Sequence domains: Peptide hormone

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided

Quick links

Citations

3 review citations

Structure and mechanism for recognition of peptide hormones by Class B G-protein-coupled receptors.
Pal et al. (2012)
2 more

1 mention without citation

Conformational Dynamics of Glucagon-like Peptide-2 with Different Electric Field.
Su et al. (2022)