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Integrative modelling of the full-length human dehydrodolichyl diphosphate synthase using a hybrid computational and experimental approach

biorxiv. 2019; 
Michal Lisnyansky?Barel, ?Su Youn?Lee, ?Ah Young?Ki, ?Noa?Kapelushnik, ?Anat?Loewenstein, ?Ka Young?Chung, ?Dina?Schneidman-Duhovny, ??View Moshe?Giladi, ?Hadas?Newman, ??View Yoni?Haitin
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Recombinant Proteins Full-length human DHDDS (UniProt Q86SQ9) was synthesized and cloned into pET-32b plasmid between the NdeI and BamHI restriction sites (GenScript, USA) as a thioredoxin (TRX) fusion protein, as previously described [17]. The construct includes a 6xHis-tag to facilitate protein purification and a TEV-protease (Tobacco Etch Virus) cleavage site to remove the 6xHis-tag and TRX fusion. Get A Quote

摘要

Dehydrodolichyl diphosphate synthase (DHDDS) and Nogo-B receptor (NgBR) form the heteromeric human?cis-prenyltransferase complex, synthesizing the precursor for the glycosyl carrier involved in N-linked protein glycosylation. In line with the important role of N-glycosylation in protein biogenesis, mutations in DHDDS, the catalytic subunit of the complex, were shown to result in human diseases. Importantly, well-characterized DHDDS homologs function as homodimers and not as heteromeric complexes. Moreover, DHDDS encompasses a C-terminal region, which does not converge with any known conserved domains. Therefore, despite the clinical importance of DHDDS, our understating of its structure-function relations rema... More

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