Ng Chai Ann, Kato Yusuke, Tanokura Masaru, Brownlee Robert T C
Department of Chemistry, La Trobe University, VIC 3086, Australia.
Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. doi: 10.1016/j.bbapap.2008.04.026. Epub 2008 May 8.
The NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics simulation suggest that the Loop I of PinA WW domain is flexible and solvent accessible, thus enabling it to bind the pS/pT-P motif. The WW domain in this structure are stabilised by a hydrophobic core. It is shown that the linker flexibility of PinA is restricted because of an alpha-helical structure in the linker region. The combination of NMR structural data and detailed Molecular Dynamics simulations enables a comprehensive structural and dynamic understanding of this protein.
本文展示了构巢曲霉PinA WW结构域的核磁共振溶液结构。PinA WW结构域的主链由一个三链反平行β折叠和一个α螺旋组成，与Ess1和Pin1相似，但没有α螺旋连接区。在核磁共振结构和分子动力学模拟中均观察到环I存在较大的均方根偏差，这表明PinA WW结构域的环I具有柔性且可与溶剂接触，从而使其能够结合pS/pT-P基序。该结构中的WW结构域通过一个疏水核心得以稳定。研究表明，由于连接区存在α螺旋结构，PinA的连接区柔性受到限制。核磁共振结构数据与详细的分子动力学模拟相结合，使得对该蛋白质的结构和动力学有了全面的理解。
