› 2lyw

Solution NMR

Intermolecular interactions between neurotensin and the third extracellular loop of human neurotensin 1 receptor

Released:
DOI: 10.2210/pdb2lyw/pdb
PDB entry 2lyw coloured by chain, ensemble of 10 models, front view.
PDB entry 2lyw coloured by chain, ensemble of 10 models, side view.
PDB entry 2lyw coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor.
Da Costa G, Bondon A, Coutant J, Curmi P, Monti JP
J Biomol Struct Dyn 31 1381-92 (2013)
PMID: 23140271

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151861 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neurotensin receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 24 amino acids
Theoretical weight: 3.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P30989 (Residues: 321-344; Coverage: 6%)
Gene names: NTRR, NTSR1
Neurotensin Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.68 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P30990 (Residues: 151-163; Coverage: 9%)
Gene name: NTS

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 50%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Not provided

Quick links

Citations

1 review citation

The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors.
Vu et al. (2021)
4 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)