Essential function of the N-termini tails of the proteasome for the gating mechanism revealed by molecular dynamics simulations
分子動力学シミュレーションを用いたプロテアソームN末端のゲート機構に対する機能発現解析
石田 恒
Ishida, Hisashi
Proteasome is involved in the degradation of proteins. Proteasome activators bind to the proteasome core particle (CP) and facilitate opening a gate of the CP, where Tyr8 and Asp9 in the N-termini tails of the CP form the ordered open gate. Four different molecular dynamics simulations were carried out: ordered- and Tyr8Gly/Asp9Gly disordered-gate models of the CP complexed with an ATP-independent PA26 and ordered- and disordered-gate models of the CP complexed with an ATP-dependent PAN-like activator. In the ordered-gate models, the substrate in the activator was more stable than that in the CP. In the disordered-gate models, the substrate in the activator was more destabilized than in the ordered-gate models. Thus, it was concluded that the dynamics of the N-termini tails entropically play a key role in the translocation of the substrate.
使用言語 : English
掲載資料名 : Proteins: Structure, Function, and Bioinformatics
: 82
: 9
ページ数 : p.1985 - 1999
発行年月 : 2014/09
出版社名 : Wiley
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キーワード : no keyword
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論文解説記事
(成果普及情報誌)
:
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登録番号 : AA20131088
抄録集掲載番号 : 42001455
論文投稿番号 : 15081
Accesses  (From Jun. 2, 2014)
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パーセンタイル:81.06
分野:Biochemistry & Molecular Biology
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