کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1179083 | 962755 | 2008 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1 Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1](/preview/png/1179083.png)
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 β-sheet and an α-helix similar to Ess1 and Pin1 without the α-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 α-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.
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1784, Issue 9, September 2008, Pages 1208–1214