2JV4

Structure Characterisation of PINA WW Domain and Comparison with other Group IV WW Domains, PIN1 and ESS1

「2JM7」から置き換えられました

2JV4 の概要

• エントリーDOI: 10.2210/pdb2jv4/pdb
• NMR情報: BMRB: 15466
• 分子名称: Peptidyl-prolyl cis/trans isomerase (1 entity in total)
• 機能のキーワード: ppiase domain, ww domain group iv, isomerase, rotamase
• 由来する生物種: Emericella nidulans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6256.97

構造登録者

Ng, C.A.,Kato, Y.,Tanokura, M.,Brownlee, R.T.C. (登録日: 2007-09-11, 公開日: 2007-10-16, 最終更新日: 2024-05-29)

主引用文献

Ng, C.A.,Kato, Y.,Tanokura, M.,Brownlee, R.T.C.
Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1
Biochim.Biophys.Acta, 1784:1208-1214, 2008

PubMed 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.

PubMed: 18503784
DOI: 10.1016/j.bbapap.2008.04.026

実験手法

SOLUTION NMR