1y32: Difference between revisions
New page: left|200px<br /> <applet load="1y32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y32" /> '''NMR structure of humanin in 30% TFE solutio... |
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[[Image:1y32.gif|left|200px]]<br /> | [[Image:1y32.gif|left|200px]]<br /><applet load="1y32" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''NMR structure of humanin in 30% TFE solution'''<br /> | '''NMR structure of humanin in 30% TFE solution'''<br /> | ||
==Overview== | ==Overview== | ||
Humanin is a newly identified 24-residue peptide that suppresses neuronal | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1Y32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1Y32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nmr solution structure]] | [[Category: nmr solution structure]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:19 2008'' | ||
Revision as of 14:01, 21 February 2008
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NMR structure of humanin in 30% TFE solution
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
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