Conformational Dynamics of the Rpt6 ATPase in Proteasome Assembly and Rpn14 Binding期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Conformational Dynamics of the Rpt6 ATPase in Proteasome Assembly and Rpn14 Binding

Authors:	Aaron Ehlinger Soyeon Park Amr Fahmy Jeffrey W Lary James L Cole Daniel Finley Kylie J Walters

Institution:	1. Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA;2. Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA;3. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA;4. Biotechnology-Bioservices Center, University of Connecticut, Storrs, CT 06269, USA

Abstract:	Download : Download high-res image (289KB) Download : Download full-size image Highlights? Proteasome ATPase Rpt6 undergoes helix-coil exchange in its C-terminal domain ? Rpt6 G^360,387A has a stabilized four-helix bundle and raised melting temperature ? Assembly chaperone Rpn14 binds selectively to the four-helix bundle Rpt6 conformer ? Rpt6 G^360,387A (rpt6AA) is synthetically defective with an rpn14 null mutation

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