Polypeptide GalNAc-Ts: from redundancy to specificity
نویسندگان
چکیده
منابع مشابه
Lectin Domains of Polypeptide GalNAc Transferases Exhibit Glycopeptide Binding Specificity*
UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (GalNAc-Ts) constitute a family of up to 20 transferases that initiate mucin-type O-glycosylation. The transferases are structurally composed of catalytic and lectin domains. Two modes have been identified for the selection of glycosylation sites by GalNAc-Ts: confined sequence recognition by the catalytic domain alone, and concerted r...
متن کاملThe lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.
Initiation of mucin-type O-glycosylation is controlled by a large family of UDP GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). Most GalNAc-transferases contain a ricin-like lectin domain in the C-terminal end, which may confer GalNAc-glycopeptide substrate specificity to the enzyme. We have previously shown that the lectin domain of GalNAc-T4 modulates its substrat...
متن کاملGrowth Factors do not regulate Golgi Complex-to-ER relocation of GalNAc-Ts in HeLa cells
Mucin-type O-glycosylation is initiated by the UDP-GalNAc polypeptide:Nacetylgalactosaminyltransferase (GalNAc-T) family of enzymes. Their activity results in the GalNAc a1-O-Thr/Ser structure, termed the Tn antigen, which is further decorated with additional sugars. In neoplastic cells, the Tn antigen is often overexpressed. Because Oglycosylation is controlled by the activity of GalNAc-Ts, th...
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In this paper, a hybrid TS-DE algorithm based on Tabu search and differential evolution algorithm is proposed to solve the reliability redundancy optimization problem. A differential evolution algorithm is embedded in Tabu search algorithm. TS is applied for searching solutions space, and DE is used for generating neighborhood solutions. The advantages of both algorithms are considered simultan...
متن کاملGlycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases.
O-Linked glycosylation is a functionally and structurally diverse type of protein modification present in many tissues and across many species. α-Dystroglycan (α-DG), a protein linked to the extracellular matrix, whose glycosylation status is associated with human muscular dystrophies, displays two predominant types of O-glycosylation, O-linked mannose (O-Man) and O-linked N-acetylgalactosamine...
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ژورنال
عنوان ژورنال: Current Opinion in Structural Biology
سال: 2019
ISSN: 0959-440X
DOI: 10.1016/j.sbi.2018.12.007