title: Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1.
abstract: 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.
authors.affiliation: Department of Chemistry, La Trobe University, VIC 3086, Australia.
authors.forename: Chai Ann
authors.initials: CA
authors.lastname: Ng
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Kato
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
authors.forename: Robert T C
authors.initials: RT
authors.lastname: Brownlee
mesh_terms: D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000201:enzymology / Q000235:genetics; D002176:Candida albicans / Q000201:enzymology / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
chemical_list: D005656:Fungal Proteins; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase