Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3

Stefan Schoebel, Wei Mi, Alexander Stein, Sergey Ovchinnikov, Ryan Pavlovicz, Frank DiMaio, David Baker, Melissa G. Chambers, Huayou Su, Dongsheng Li, Tom A. Rapoport () and Maofu Liao ()
Additional contact information
Stefan Schoebel: Harvard Medical School
Wei Mi: Harvard Medical School
Alexander Stein: Max Planck Institute for Biophysical Chemistry
Sergey Ovchinnikov: Institute for Protein Design, University of Washington
Ryan Pavlovicz: Institute for Protein Design, University of Washington
Frank DiMaio: Institute for Protein Design, University of Washington
David Baker: Institute for Protein Design, University of Washington
Melissa G. Chambers: Harvard Medical School
Huayou Su: National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology
Dongsheng Li: National Lab for Parallel and Distributed Processing (PDL), School of Computer Science, National University of Defense Technology
Tom A. Rapoport: Harvard Medical School
Maofu Liao: Harvard Medical School

Nature, 2017, vol. 548, issue 7667, 352-355

Abstract: The structure of yeast Hrd1 in complex with Hrd3 shows that Hrd1 forms an aqueous cavity with a lateral seal within the endoplasmic reticulum membrane, shedding light on how misfolded proteins are transported out of the endoplasmic reticulum.

Date: 2017
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DOI: 10.1038/nature23314

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