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...
المؤلفون الرئيسيون: | 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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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
Cell Press
2020
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مواد مشابهة
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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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