2dez
From Proteopedia
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|PDB= 2dez |SIZE=350|CAPTION= <scene name='initialview01'>2dez</scene> | |PDB= 2dez |SIZE=350|CAPTION= <scene name='initialview01'>2dez</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2df0|2DF0]] | ||
| + | |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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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nygaard, R.]] | [[Category: Nygaard, R.]] | ||
| - | [[Category: NH2]] | ||
[[Category: helix]] | [[Category: helix]] | ||
[[Category: neuropeptide]] | [[Category: neuropeptide]] | ||
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[[Category: pp-fold]] | [[Category: pp-fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:33:51 2008'' |
Revision as of 23:33, 30 March 2008
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| Ligands: | |||||||
| Related: | 2DF0
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 of sequence from [1]. 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 Mon Mar 31 02:33:51 2008
Categories: Single protein | Nygaard, R. | Helix | Neuropeptide | Peptide | Pp-fold
