1y32
From Proteopedia
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NMR structure of humanin in 30% TFE solution
Contents |
Overview
Humanin is a newly identified 24-residue peptide that suppresses neuronal, cell death caused by a wide spectrum of familial Alzheimer's disease genes, and the beta-amyloid peptide. In this study, NMR and circular dichroism, studies of synthetic humanin in aqueous and 30% 2,2,2-trifluoroethanol, (TFE) solutions are reported. In aqueous solution, humanin exists, predominantly in an unstructured conformation in equilibrium with, turn-like structures involving residues Gly5 to Leu10 and Glu15 to Leu18, providing indication of nascent helix. In the less polar environment of, 30% TFE, humanin readily adopts helical structure with long-range order, spanning residues Gly5 to Leu18. Comparative 3D modeling studies and, topology predictions are in qualitative agreement with the experimental, findings in both environments. Our studies reveal a flexible peptide in, aqueous environment, which is free to interact with possible receptors, that mediate its action, but may also acquire a helical conformation, necessary for specific interactions and/or passage through membranes.
Disease
Known disease associated with this structure: Hartnup disorder OMIM:[608893]
About this Structure
1Y32 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity., Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M, Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:15721287
Page seeded by OCA on Mon Nov 12 20:14:18 2007
