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

Authors :: Nyggard, Rie
Nielbo, Steen
Schwartz, Thue W.
Poulsen, Flemming M.
Source :: Biochemistry. July 11, 2006, Vol. 45 Issue 27, p8350, 8 p.
Publication Year :: 2006
Abstract: The NMR analysis is used to explain the highly ordered, back-folded structure for human polypeptide YY (PYY) and human PYY3-36, which was found to be exactly similar to the classical pancreatic polypeptide (PP)-fold solution structure. The analysis proves that the PP-fold is extremely essential for establishing interactions with two subsites in the receptor for binding the N- and C-terminal ends of PYY, as both the segments are characterized by larger dynamics.

Subjects :: Polypeptides -- Structure
Polypeptides -- Chemical properties
Nuclear magnetic resonance -- Analysis
Weight reducing preparations -- Structure
Weight reducing preparations -- Chemical properties
Protein folding -- Research
Biological sciences
Chemistry

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