Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose:glycoprotein glucosyltransferase
UDP-glucose:glycoprotein glucosyltransferase (UGGT) flags misfolded glycoproteins for ER retention. We report crystal structures of full-length Chaetomium thermophilum UGGT (CtUGGT), two CtUGGT double-cysteine mutants, and its TRXL2 domain truncation (CtUGGT-ΔTRXL2). CtUGGT molecular dynamics (MD) s...
Κύριοι συγγραφείς: | Modenutti, CP, Blanco Capurro, JI, Ibba, R, Alonzi, DS, Song, MN, Vasiljević, S, Kumar, A, Chandran, AV, Tax, G, Marti, L, Hill, JC, Lia, A, Hensen, M, Waksman, T, Rushton, J, Rubichi, S, Santino, A, Martí, MA, Zitzmann, N, Roversi, P |
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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
Cell Press
2020
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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Clamping, bending, and twisting inter-domain motions in the misfold-recognising portion of UDP-glucose: glycoprotein glucosyl-transferase
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