The protein proteinase inhibitor from kidney bean (isoinhibitor, pI 4.3) is a double-headed inhibitor with independent reactive sites for trypsin and chymotrypsin. The reactive site of the inhibitor for trypsin is Lys (22)- Ser (23) in the sequense ...-Lys-Ser-Ile-Pro-Ala-Glx-Cys-Arg-..., the reactive site for chymotrypsin is Leu (64)-Ser (65) in the sequence ...-Thr-Leu-Ser-Ile-Pro-Ala-Glx-Cys-Arg-... .
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January 2025
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA. Electronic address:
High-risk human papillomavirus E6 oncoprotein is a model system for the recognition and degradation of cellular p53 tumor suppressor protein. There remains a gap in the understanding of the ubiquitin transfer reaction, including placement of the E6AP catalytic HECT domain of the ligase concerning the p53 substrate and how E6 itself is protected from ubiquitination. We determined the cryoelectron microscopy (cryo-EM) structure of the E6AP/E6/p53 complex, related the structure to in vivo modeling of the tri-molecular complex, and identified structural interactions associated with activation of the ubiquitin ligase function.
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April 2024
Institut für Parasitologie, Biomedizinisches Forschungszentrum Seltersberg (BFS), Justus Liebig Universitaet Giessen, Giessen, Germany.
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Sci Rep
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Laboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, Wita Stwosza 59, Gdansk, 80-308, Poland.
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CSIC - Insituto de Catálisis y Petroleoquímica, Madrid, Spain.
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