Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1.,Ng CA, Kato Y, Tanokura M, Brownlee RT Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. Epub 2008 May 8. PMID:18503784[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ng CA, Kato Y, Tanokura M, Brownlee RT. Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1. Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. Epub 2008 May 8. PMID:18503784 doi:10.1016/j.bbapap.2008.04.026