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2dez

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[[Image:2dez.jpg|left|200px]]
[[Image:2dez.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_2dez| PDB=2dez | SCENE= }}
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|RELATEDENTRY=[[2df0|2DF0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dez OCA], [http://www.ebi.ac.uk/pdbsum/2dez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dez RCSB]</span>
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'''Structure of human PYY'''
'''Structure of human PYY'''
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==About this Structure==
==About this Structure==
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2DEZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DEZ OCA].
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2DEZ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DEZ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Nygaard, R.]]
[[Category: Nygaard, R.]]
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[[Category: helix]]
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[[Category: Helix]]
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[[Category: neuropeptide]]
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[[Category: Neuropeptide]]
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[[Category: peptide]]
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[[Category: Peptide]]
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[[Category: pp-fold]]
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[[Category: Pp-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:17:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:33:51 2008''
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Revision as of 21:18, 3 May 2008

Template:STRUCTURE 2dez

Structure of human PYY


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

2DEZ 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 00:17:59 2008

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