Clamping, bending, and twisting inter-domain motions in the misfold-recognising portion of UDP-glucose: glycoprotein glucosyl-transferase
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, Capurro, JIB, 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-recognizing portion of UDP-glucose:glycoprotein glucosyltransferase
حسب: Modenutti, CP, وآخرون
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Rescue of secretion of rare-disease associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells
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Is aberrant N-glucosylation relevant to recognise anti-MOG antibodies in Rett syndrome?
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Glucosylated free oligosaccharides are biomarkers of endoplasmic- reticulum alpha-glucosidase inhibition.
حسب: Alonzi, D, وآخرون
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Genome-wide analysis of UDP-glycosyltransferase gene family and identification of members involved in flavonoid glucosylation in Chinese bayberry (Morella rubra)
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