纽蛋白尾部结构域的主链1H、13C和15N核磁共振信号归属
Backbone 1H, 13C, and 15N NMR assignments of the tail domain of vinculin.
作者信息
Palmer Sean M, Campbell Sharon L
机构信息
Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
出版信息
Biomol NMR Assign. 2008 Jun;2(1):69-71. doi: 10.1007/s12104-008-9087-7. Epub 2008 Apr 4.
PMID:19636928
Abstract
Vinculin is an essential protein involved in linking the actin cytoskeleton to sites of cell-cell and cell-matrix adhesion. Here we report the majority of the backbone 1H(N), 15N, 13C(alpha), 13CO, and side chain 13C(beta) NMR resonance assignments of the actin binding tail domain of vinculin (Vt).
摘要
纽蛋白是一种重要蛋白质，参与将肌动蛋白细胞骨架与细胞间和细胞-基质黏附位点相连。在此我们报告纽蛋白（Vt）肌动蛋白结合尾部结构域的大部分主链1H(N)、15N、13C(α)、13CO以及侧链13C(β)核磁共振共振归属。
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