1Y32

NMR structure of humanin in 30% TFE solution

Summary for 1Y32

• Entry DOI: 10.2210/pdb1y32/pdb
• Descriptor: Humanin (1 entity in total)
• Functional Keywords: humanin, nmr solution structure, alzheimer's disease, neuroprotection, unknown function
• Cellular location: Secreted: Q8IVG9
• Total number of polymer chains: 1
• Total formula weight: 2691.26

Authors

Benaki, D.,Zikos, C.,Evangelou, A.,Livaniou, E.,Vlassi, M.,Mikros, E.,Pelecanou, M. (deposition date: 2004-11-23, release date: 2005-02-22, Last modification date: 2024-05-22)

Primary citation

Benaki, D.,Zikos, C.,Evangelou, A.,Livaniou, E.,Vlassi, M.,Mikros, E.,Pelecanou, M.
Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity.
Biochem.Biophys.Res.Commun., 329:152-160, 2005

PubMed Abstract: 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.

PubMed: 15721287
DOI: 10.1016/j.bbrc.2005.01.100

Experimental method

SOLUTION NMR