2df0: Difference between revisions
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'''Solution structure of human PYY3-36''' | '''Solution structure of human PYY3-36''' | ||
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==About this Structure== | ==About this Structure== | ||
2DF0 is a [[Single protein]] structure | 2DF0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DF0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nygaard, R.]] | [[Category: Nygaard, R.]] | ||
[[Category: | [[Category: Amphipathic]] | ||
[[Category: | [[Category: Helix]] | ||
[[Category: | [[Category: Neuropeptide]] | ||
[[Category: | [[Category: Peptide]] | ||
[[Category: | [[Category: Pp-fold]] | ||
[[Category: | [[Category: Pyy]] | ||
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Revision as of 21:18, 3 May 2008
Solution structure of human PYY3-36
Overview
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.
About this Structure
2DF0 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
The PP-fold solution structure of human polypeptide YY and human PYY3-36 as determined by NMR., Nygaard R, Nielbo S, Schwartz TW, Poulsen FM, Biochemistry. 2006 Jul 11;45(27):8350-7. PMID:16819834 Page seeded by OCA on Sun May 4 00:18:10 2008