Drescher Malte, Veldhuis Gertjan, van Rooijen Bart D, Milikisyants Sergey, Subramaniam Vinod, Huber Martina
Department of Molecular Physics, Leiden University, P.O. Box 9504, 2300 RA Leiden, The Netherlands.
J Am Chem Soc. 2008 Jun 25;130(25):7796-7. doi: 10.1021/ja801594s. Epub 2008 May 31.
alpha-Synuclein (alphaS) is the main component of Lewy bodies from Parkinson's disease. That alphaS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of alphaS sheds light on the most likely structure. For alphaS bound to vesicles large enough to accommodate also the extended conformation, an antiparallel helix conformation is found. This suggests that the bent structure shown is the preferred conformation of alphaS on membranes.
α-突触核蛋白（αS）是帕金森病路易小体的主要成分。αS与膜结合这一点是已知的，但其所采用的构象仍不清楚。对αS的双自旋标记变体进行脉冲电子顺磁共振揭示了最可能的结构。对于与足够大以容纳伸展构象的囊泡结合的αS，发现了一种反平行螺旋构象。这表明所示的弯曲结构是αS在膜上的优选构象。
