Smyd3 open & closed lock mechanism for substrate recruitment: The hinge motion of C-terminal domain inferred from μ-second molecular dynamics simulations
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- 作者：Balasubramanian Chandramoulia ; bala.chandramouli@sns.it" class="auth_mail" title="E-mail the corresponding author ; Valentina Silvestrib ; Marco Scarnoc ; Laura Ottinib ; Giovanni Chillemic ; giochillemi@gmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：SET ; Suppressor of variegation ; Enhancer of Zeste ; Trithorax ; MYND ; Myeloid-Nervy-DEAF1 ; siRNA ; small interfering RNA ; VEGFR1 ; vascular endothelial growth factor receptor-1 ; MD ; molecular dynamics ; HKMT ; histone lysine methyltranferase ; RMSD ; root-mean square deviation ; RMSF ; root-mean-square fluctuation ; SASA ; solvent accessible surface area
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：1860
- 期：7
- 页码：1466-1474
- 全文大小：2444 K
文摘
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Smyd3 exhibits an open and closed conformation in apo and holo states.
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Adomet binding locks Smyd3 in a closed conformation.
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CTD hinge motion is important for stabilizing the substrate binding crevice.