2df0
From Proteopedia
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|PDB= 2df0 |SIZE=350|CAPTION= <scene name='initialview01'>2df0</scene> | |PDB= 2df0 |SIZE=350|CAPTION= <scene name='initialview01'>2df0</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=[[2dez|2DEZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2df0 OCA], [http://www.ebi.ac.uk/pdbsum/2df0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2df0 RCSB]</span> | ||
}} | }} | ||
| Line 22: | Line 25: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Nygaard, R.]] | [[Category: Nygaard, R.]] | ||
| - | [[Category: NH2]] | ||
[[Category: amphipathic]] | [[Category: amphipathic]] | ||
[[Category: helix]] | [[Category: helix]] | ||
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[[Category: pyy]] | [[Category: pyy]] | ||
| - | ''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 02:33:50 2008'' |
Revision as of 23:33, 30 March 2008
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| Ligands: | |||||||
| Related: | 2DEZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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 02:33:50 2008
Categories: Single protein | Nygaard, R. | Amphipathic | Helix | Neuropeptide | Peptide | Pp-fold | Pyy
