Effects of interface mutations on the dimerization of alanine glyoxylate aminotransferase and implications in the mistargeting of the pathogenic variants F152I and I244T

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• 作者：Mirco Dindo^a ; Riccardo Montioli^a ; Mirko Busato^b ; Alejandro Giorgetti^b ; Barbara Cellini^a ; Carla Borri Voltattorni^a ; ^{carla.borrivoltattorni@univr.it}
• 关键词：Primary hyperoxaluria type I ; Human alanine glyoxylate aminotransferase ; Interface hot spots ; Protein dimerization ; Molecular dynamics ; Protein mistargeting
• 刊名：Biochimie
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：131
• 期：Complete
• 页码：137-148
• 全文大小：1848 K
• 卷排序：131

文摘

Identification of the main interface hot-spot of AGT-Mi. Expression and purification of an engineered soluble monomeric form of AGT-Mi. Determination of the kinetics of the dimerization process of monomeric AGT-Mi. Monomeric AGT-Mi binds PLP but does not display catalytic activity. Proposal of a model explaining the mistargeting of the variants F152I-Mi and I244T-Mi.