The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR

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Standard

The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. / Nygaard, Rie; Nielbo, Steen; Schwartz, Thue W; Poulsen, Flemming M.

In: Biochemistry, Vol. 45, No. 27, 2006, p. 8350-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nygaard, R, Nielbo, S, Schwartz, TW & Poulsen, FM 2006, 'The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR', Biochemistry, vol. 45, no. 27, pp. 8350-7. https://doi.org/10.1021/bi060359l

APA

Nygaard, R., Nielbo, S., Schwartz, T. W., & Poulsen, F. M. (2006). The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. Biochemistry, 45(27), 8350-7. https://doi.org/10.1021/bi060359l

Vancouver

Nygaard R, Nielbo S, Schwartz TW, Poulsen FM. The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. Biochemistry. 2006;45(27):8350-7. https://doi.org/10.1021/bi060359l

Author

Nygaard, Rie ; Nielbo, Steen ; Schwartz, Thue W ; Poulsen, Flemming M. / The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR. In: Biochemistry. 2006 ; Vol. 45, No. 27. pp. 8350-7.

Bibtex

@article{0c292c9070ec11dcbee902004c4f4f50,
title = "The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR",
abstract = "PYY3-36 is a biopharmaceutical antiobesity agent under development as well as an endogenous satiety hormone, which is generated by dipeptidyl peptidase-IV digestion of polypetide YY (PYY), and in contrast to the parent hormone, PYY is highly selective for the Y2 versus the Y1 receptor. NMR analysis revealed a highly ordered, back-folded structure for human PYY in aqueous solution similar to the classical PP-fold structure of pancreatic polypeptide. The NMR analysis of PYY3-36 also showed a folded structure resembling a PP-fold, which however was characterized by far fewer long distance NOEs than the PP-fold observed in the full-length peptide. This suggests that either a conformational change has occurred in the N-terminal segment of PYY3-36 or that this segments is characterized by larger dynamics. The study supports the notion that the PP-fold is crucial for establishing simultaneous interactions with two subsites in the receptor for binding of, respectively, the N- and C-terminal ends of PYY. The Y2 receptor only requires recognition of the C-terminal segment of the molecule as displayed by the Y2 selective PYY3-36.",
author = "Rie Nygaard and Steen Nielbo and Schwartz, {Thue W} and Poulsen, {Flemming M}",
note = "Keywords: Amino Acid Sequence; Animals; COS Cells; Cercopithecus aethiops; Humans; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptide YY; Protein Conformation; Protein Folding; Receptors, Gastrointestinal Hormone; Solutions; Transfection",
year = "2006",
doi = "10.1021/bi060359l",
language = "English",
volume = "45",
pages = "8350--7",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "27",

}

RIS

TY - JOUR

T1 - The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR

AU - Nygaard, Rie

AU - Nielbo, Steen

AU - Schwartz, Thue W

AU - Poulsen, Flemming M

N1 - Keywords: Amino Acid Sequence; Animals; COS Cells; Cercopithecus aethiops; Humans; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptide YY; Protein Conformation; Protein Folding; Receptors, Gastrointestinal Hormone; Solutions; Transfection

PY - 2006

Y1 - 2006

N2 - PYY3-36 is a biopharmaceutical antiobesity agent under development as well as an endogenous satiety hormone, which is generated by dipeptidyl peptidase-IV digestion of polypetide YY (PYY), and in contrast to the parent hormone, PYY is highly selective for the Y2 versus the Y1 receptor. NMR analysis revealed a highly ordered, back-folded structure for human PYY in aqueous solution similar to the classical PP-fold structure of pancreatic polypeptide. The NMR analysis of PYY3-36 also showed a folded structure resembling a PP-fold, which however was characterized by far fewer long distance NOEs than the PP-fold observed in the full-length peptide. This suggests that either a conformational change has occurred in the N-terminal segment of PYY3-36 or that this segments is characterized by larger dynamics. The study supports the notion that the PP-fold is crucial for establishing simultaneous interactions with two subsites in the receptor for binding of, respectively, the N- and C-terminal ends of PYY. The Y2 receptor only requires recognition of the C-terminal segment of the molecule as displayed by the Y2 selective PYY3-36.

AB - PYY3-36 is a biopharmaceutical antiobesity agent under development as well as an endogenous satiety hormone, which is generated by dipeptidyl peptidase-IV digestion of polypetide YY (PYY), and in contrast to the parent hormone, PYY is highly selective for the Y2 versus the Y1 receptor. NMR analysis revealed a highly ordered, back-folded structure for human PYY in aqueous solution similar to the classical PP-fold structure of pancreatic polypeptide. The NMR analysis of PYY3-36 also showed a folded structure resembling a PP-fold, which however was characterized by far fewer long distance NOEs than the PP-fold observed in the full-length peptide. This suggests that either a conformational change has occurred in the N-terminal segment of PYY3-36 or that this segments is characterized by larger dynamics. The study supports the notion that the PP-fold is crucial for establishing simultaneous interactions with two subsites in the receptor for binding of, respectively, the N- and C-terminal ends of PYY. The Y2 receptor only requires recognition of the C-terminal segment of the molecule as displayed by the Y2 selective PYY3-36.

U2 - 10.1021/bi060359l

DO - 10.1021/bi060359l

M3 - Journal article

C2 - 16819834

VL - 45

SP - 8350

EP - 8357

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 27

ER -

ID: 1205051