Direct Evidence of Coexisting Horseshoe and Extended Helix Conformations of Membrane-Bound Alpha-Synuclein

被引：56

作者：

Robotta, Marta ^{[4
]}

Braun, Patrick ^{[4
]}

van Rooijen, Bart ^{[1
,2
]}

Subramaniam, Vinod ^{[1
,2
]}

Huber, Martina ^{[3
]}

Drescher, Malte ^{[4
]}

机构：

[1] Univ Twente, MESA Inst Nanotechnol, NL-7500 AE Enschede, Netherlands

[2] Univ Twente, MIRA Inst Biomed Technol & Tech Med, NL-7500 AE Enschede, Netherlands

[3] Leiden Univ, Leiden Inst Phys, NL-2300 RA Leiden, Netherlands

[4] Univ Konstanz, Dept Chem, D-78457 Constance, Germany

来源：

CHEMPHYSCHEM | 2011年 / 12卷 / 02期

关键词：

electron paramagnetic resonance; membranes; proteins; site-directed spin labeling; vesicles; DYNAMICS; BINDING; PROTEIN; VESICLES; DISEASE;

D O I：

10.1002/cphc.201000815

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Good luck! The physiologically relevant conformation of membrane-bound α-Synuclein (αS) can be either a horseshoe or an extended helix structure. Experimental data obtained by site-directed spin labeling in combination with pulsed electron paramagnetic resonance provide compelling evidence of the coexistence of the horseshoe structure and an extended helix of αS bound to a membrane surface, and potentially resolve the debate on the structure of membrane-bound αS. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：267 / 269

页数：3

共 31 条

[1] Copper binding properties of membrane-bound alpha-synuclein
Lucas, Heather R.
Jackson, Mark S.
Lee, Jennifer C.
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2009, 237
[2] Characterization of Membrane-Bound Alpha-Synuclein with the Thiocyanate Vibrational Probe Group
Kostas, Franklin A.
Shroff, Kavita
Fiore, Kristen E.
Konstantinovsky, Daniel M.
Londergan, Casey H.
BIOPHYSICAL JOURNAL, 2018, 114 (03) : 616A - 617A
[3] Using thiocyanate probes to examine the membrane-bound structures of alpha-synuclein
Stark, Melanie R.
Qaraqe, Tala
Ryan, Abby
Shattuck, Vera
Minyety, Perla Villegas
Londergan, Casey H.
BIOPHYSICAL JOURNAL, 2024, 123 (03) : 214A - 214A
[4] Membrane-Bound Structures of Alpha-Synuclein Revealed by Infrared Spectroscopy of Cyanylated Cysteine
Vienneau, Alice R.
Londergan, Casey H.
BIOPHYSICAL JOURNAL, 2013, 104 (02) : 51A - 51A
[5] Distinguishing Different Conformations of Membrane-Bound Alpha-Synucl Synuclein through Distance Measurements
Williams, Brandon
Sarver, Jessica
FASEB JOURNAL, 2021, 35
[6] Copper(II) enhances membrane-bound α-synuclein helix formation
Lucas, Heather R.
Lee, Jennifer C.
METALLOMICS, 2011, 3 (03) : 280 - 283
[7] Studying the Membrane-Bound Conformation of Alpha-Synuclein using a Model Transmembrane Peptide System in a Lipid Bilayer
Lobel, Graham P.
Vienneau, Alice R.
Londergan, Casey H.
BIOPHYSICAL JOURNAL, 2015, 108 (02) : 559A - 559A
[8] Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore
Hoogerheide, David P.
Rostovtseva, Tatiana K.
Bezrukov, Sergey M.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2021, 1863 (09):
[9] Insights on Channel-Like Activity of Membrane Bound Alpha-Synuclein
Tosatto, Laura
Plotegher, Nicoletta
Tessari, Isabella
Bisaglia, Marco
Bubacco, Luigi
Dalla Serra, Mauro
BIOPHYSICAL JOURNAL, 2010, 98 (03) : 109A - 109A
[10] Vesicle-Bound Alpha-Synuclein: Are the Helices Anti-Parallel or Extended?
Drescher, Malte
van Rooijen, Bart D.
Veldhuis, Gertjan
Godschalk, Frans
Milikisyants, Sergey
Subramaniam, Vinod
Huber, Martina
BIOPHYSICAL JOURNAL, 2010, 98 (03) : 258A - 258A

← 1 2 3 4 →