In-silico structural analysis of E509K mutation in LARGE and T192M mutation in Alpha Dystroglycan in the inhibition of glycosylation of Alpha Dystroglycan by LARGE
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- 作者：Simanti Bhattacharya simanti.bhattacharya@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Amit Das amit.das.ku@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Angshuman Bagchi ; angshu@klyuniv.ac.in" class="auth_mail" title="E-mail the corresponding author ; angshuman_bagchi@yahoo.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：DMD ; Duchenne Muscular Dystrophy ; α-DG ; Alpha Dystroglycan ; DAPC ; Dystrophin Associated Protein Complex ; MDDGC9 ; Muscular Dystrophy Dystroglycanopathy type C9 ; OMIM ; Online Mendelian Inheritance in Man ; EC ; Enzyme Commission number ; MDDGB6 ; Muscular Dystrophy Dystroglycanopathy type B6 ; GlcA ; glucuronic acid ; Xyl ; Xylosyl moety ; PDB ; Protein Data Bank ; WT ; Wild type ; MT ; Mutant
- 刊名：Computational Biology and Chemistry
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：64
- 期：Complete
- 页码：313-321
- 全文大小：2009 K
文摘
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E509K mutation of LARGE causes MDDGB6.
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Structure of LARGE is altered due to this E509K mutation.
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Glucuronic acid binding ability of LARGE is weakened due to E509K mutation.
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E509K mutation hampers the interaction between LARGE and Alpha Dystroglycan.