Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1179083 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2008 | 7 Pages |
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.