2gd3

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NMR structure of S14G-humanin in 30% TFE solution

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The NMR solution study of Ser14Gly-humanin (S14G-HN), a 1000-fold more potent derivative of humanin (HN), is reported. HN is 24-residue peptide that selectively suppresses neuronal cell death caused by Alzheimer's disease (AD)-specific insults and offers hope for the development of a cure against AD. In aqueous solution the NMR data show that S14G-HN is a flexible peptide with turn-like structures in its conformational ensemble distributed over an extensive part of its sequence from Pro3 to Glu15. In the more lipophilic environment of 30% TFE, an alpha-helical structure spanning residues Phe6 to Thr13 is identified. Comparison of these findings to the NMR structure of the parent HN and to existing structure-function relationship literature data outlines the important for activity structural features for this class of neuroprotective peptides, and brings forth flexibility as an important characteristic that may facilitate interactions with functional counterparts of the neuroprotection pathway.

Disease

Known disease associated with this structure: Hartnup disorder OMIM:[608893]

About this Structure

2GD3 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Solution structure of Ser14Gly-humanin, a potent rescue factor against neuronal cell death in Alzheimer's disease., Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M, Biochem Biophys Res Commun. 2006 Oct 20;349(2):634-42. Epub 2006 Aug 23. PMID:16945331

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