1xq8

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[[Image:1xq8.gif|left|200px]]
[[Image:1xq8.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1xq8", creates the "Structure Box" on the page.
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|GENE= SNCA, NACP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1xq8| PDB=1xq8 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xq8 OCA], [http://www.ebi.ac.uk/pdbsum/1xq8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xq8 RCSB]</span>
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'''Human micelle-bound alpha-synuclein'''
'''Human micelle-bound alpha-synuclein'''
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[[Category: Nussbaum, R L.]]
[[Category: Nussbaum, R L.]]
[[Category: Ulmer, T S.]]
[[Category: Ulmer, T S.]]
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[[Category: micelle-bound helix]]
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[[Category: Micelle-bound helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:21:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:06 2008''
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Revision as of 12:21, 3 May 2008

Template:STRUCTURE 1xq8

Human micelle-bound alpha-synuclein


Overview

Misfolding of the protein alpha-synuclein (aS), which associates with presynaptic vesicles, has been implicated in the molecular chain of events leading to Parkinson's disease. Here, the structure and dynamics of micelle-bound aS are reported. Val3-Val37 and Lys45-Thr92 form curved alpha-helices, connected by a well ordered, extended linker in an unexpected anti-parallel arrangement, followed by another short extended region (Gly93-Lys97), overlapping the recently identified chaperone-mediated autophagy recognition motif and a highly mobile tail (Asp98-Ala140). Helix curvature is significantly less than predicted based on the native micelle shape, indicating a deformation of the micelle by aS. Structural and dynamic parameters show a reduced helical content for Ala30-Val37. A dynamic variation in interhelical distance on the microsecond timescale is complemented by enhanced sub-nanosecond timescale dynamics, particularly in the remarkably glycine-rich segments of the helices. These unusually rich dynamics may serve to mitigate the effect of aS binding on membrane fluidity. The well ordered conformation of the helix-helix connector indicates a defined interaction with lipidic surfaces, suggesting that, when bound to larger diameter synaptic vesicles, it can act as a switch between this structure and a previously proposed uninterrupted helix.

About this Structure

1XQ8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and dynamics of micelle-bound human alpha-synuclein., Ulmer TS, Bax A, Cole NB, Nussbaum RL, J Biol Chem. 2005 Mar 11;280(10):9595-603. Epub 2004 Dec 22. PMID:15615727 Page seeded by OCA on Sat May 3 15:21:42 2008

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