PDBsum entry 2oon

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protein links
Hormone PDB id
Protein chain
37 a.a. *
* Residue conservation analysis
PDB id:
Name: Hormone
Title: Structure of ala14-pyy in aqueous solution
Structure: Peptide yy. Chain: a. Synonym: pyy, peptide tyrosine tyrosine. Engineered: yes. Mutation: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Gene: pyy. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: O.Zerbe,A.Neumoin,J.Mares
Key ref: A.Neumoin et al. (2007). Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin. J Am Chem Soc, 129, 8811-8817. PubMed id: 17580866 DOI: 10.1021/ja0716960
26-Jan-07     Release date:   25-Dec-07    
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Protein chain
Pfam   ArchSchema ?
P68005  (PYY_PIG) -  Peptide YY
36 a.a.
37 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     eating behavior   1 term 
  Biochemical function     hormone activity     2 terms  


DOI no: 10.1021/ja0716960 J Am Chem Soc 129:8811-8817 (2007)
PubMed id: 17580866  
Probing the formation of stable tertiary structure in a model miniprotein at atomic resolution: determinants of stability of a helical hairpin.
A.Neumoin, J.Mares, M.Lerch-Bader, R.Bader, O.Zerbe.
The minimal model system to study the basic principles of protein folding is the hairpin. The formation of beta-hairpins, which are the basic components of antiparallel beta-sheets, has been studied extensively in the past decade, but much less is known about helical hairpins. Here, we probe hairpin formation between a polyproline type-II helix and an alpha-helix as present in the natural miniprotein peptide YY (PYY). Both turn sequence and interactions of aromatic side chains from the C-terminal alpha-helix with the pockets formed by N-terminal Pro residues are shown by site-directed mutagenesis and solution NMR spectroscopy in different solvent systems to be important determinants of backbone dynamics and hairpin stability, suggesting a close analogy with some beta-hairpin structures. It is shown that multiple relatively weak contacts between the helices are necessary for the formation of the helical hairpin studied here, whereas the type-I beta-turn acts like a hinge, which through certain single amino acid substitutions is destabilized such that hairpin formation is completely abolished. Denaturation and renaturation of tertiary structure by temperature or cosolvents were probed by measuring changes of chemical shifts. Folding of PYY is both reversible and cooperative as inferred from the sigmoidal denaturation curves displayed by residues at the interface of the helical hairpin. Such miniproteins thus feature an important hallmark of globular proteins and should provide a convenient system to study basic aspects of helical hairpin folding that are complementary to those derived from studies of beta-hairpins.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20853314 S.L.Pedersen, P.G.Sasikumar, S.Chelur, B.Holst, A.Artmann, K.J.Jensen, and N.Vrang (2010).
Peptide hormone isoforms: N-terminally branched PYY3-36 isoforms give improved lipid and fat-cell metabolism in diet-induced obese mice.
  J Pept Sci, 16, 664-673.  
19278658 N.Keller, J.Mares, O.Zerbe, and M.G.Grütter (2009).
Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation.
  Structure, 17, 438-448.
PDB code: 2k7z
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