› 2rlk

Solution NMR

Refined solution structure of porcine peptide YY (PYY)

Released:
DOI: 10.2210/pdb2rlk/pdb
PDB entry 2rlk coloured by chain, ensemble of 20 models, front view.
PDB entry 2rlk coloured by chain, ensemble of 20 models, side view.
PDB entry 2rlk coloured by chain, ensemble of 20 models, top view.
Source organism: Sus scrofa
Primary publication:
Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin.
Neumoin A, Mares J, Lerch-Bader M, Bader R, Zerbe O
J Am Chem Soc 129 8811-7 (2007)
PMID: 17580866

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159268 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide YY Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.25 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P68005 (Residues: 1-36; Coverage: 100%)
Gene name: PYY
Sequence domains: Pancreatic hormone peptide

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Force-field minimization using AMBER
Expression system: Escherichia coli BL21

Quick links

Citations

6 citation in other articles

Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation.
Keller et al. (2009)
5 more

3 mentions without citation

Infrared study of the folding mechanism of a helical hairpin: porcine PYY.
Waegele et al. (2010)
2 more