1qfa

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STRUCTURE OF A NEUROPEPTIDE Y Y2 AGONIST

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The solution structure and self-association behaviour of a 13 residue, peptide analogue of the C-terminal region of human neuropeptide Y (NPY), have been investigated. NMR analysis of Ac[Leu(28,31)]NPY(24-36), a potent, Y2 receptor agonist, shows that it is unstructured in aqueous solution at, 5-20 degrees C, but forms a well-defined helix (encompassing residues, 25-35) in 40% trifluoroethanol/water at 20 degrees C. Sedimentation, experiments show that, in contrast to many peptides in aqueous, trifluoroethanol, Ac[Leu(28,31)]NPY(24-36) associates to form a trimer or, more likely, a tetramer in 40% trifluoroethanol, even though it is, monomeric in water. This is consistent with the observation of, inter-molecular nuclear Overhauser enhancements in trifluoroethanol., Possible models of the associated form that are consistent with the NMR, data are described. The relevance of the helical structure observed in, trifluoroethanol to the structure of this peptide bound to the NPY Y2, receptor is discussed.

Disease

Known diseases associated with this structure: Myelokathexis, isolated OMIM:[162643], WHIM syndrome OMIM:[162643]

About this Structure

1QFA is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

Helical structure and self-association in a 13 residue neuropeptide Y Y2 receptor agonist: relationship to biological activity., Barnham KJ, Catalfamo F, Pallaghy PK, Howlett GJ, Norton RS, Biochim Biophys Acta. 1999 Nov 16;1435(1-2):127-37. PMID:10561544

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