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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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

•: E509K mutation of LARGE causes MDDGB6.
•: Structure of LARGE is altered due to this E509K mutation.
•: Glucuronic acid binding ability of LARGE is weakened due to E509K mutation.
•: E509K mutation hampers the interaction between LARGE and Alpha Dystroglycan.