1y32

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[[Image:1y32.gif|left|200px]]
[[Image:1y32.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1y32", creates the "Structure Box" on the page.
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{{STRUCTURE_1y32| PDB=1y32 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB]</span>
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'''NMR structure of humanin in 30% TFE solution'''
'''NMR structure of humanin in 30% TFE solution'''
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==About this Structure==
==About this Structure==
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1Y32 is a [[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].
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1Y32 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].
==Reference==
==Reference==
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[[Category: Vlassi, M.]]
[[Category: Vlassi, M.]]
[[Category: Zikos, C.]]
[[Category: Zikos, C.]]
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[[Category: alzheimer's disease]]
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[[Category: Alzheimer's disease]]
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[[Category: humanin]]
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[[Category: Humanin]]
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[[Category: neuroprotection]]
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[[Category: Neuroprotection]]
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[[Category: nmr solution structure]]
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[[Category: Nmr solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:49:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:08 2008''
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Revision as of 12:49, 3 May 2008

Template:STRUCTURE 1y32

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.

About this Structure

1Y32 is a Single protein structure. 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 Sat May 3 15:49:33 2008

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