Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of Ap₄A

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• 作者：Rafał Dolot ; ^{rdolot@cbmm.lodz.pl" class="auth_mail" title="E-mail the corresponding author} ; Renata Kaczmarek ; Aleksandra Sęda ; Agnieszka Krakowiak ; Janina Baraniak ; Barbara Nawrot
• 关键词：Histidine triad nucleotide-binding protein ; Ap4A analog ; Protein crystallography
• 刊名：International Journal of Biological Macromolecules
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：87
• 期：Complete
• 页码：62-69
• 全文大小：4064 K

文摘

Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch in the histidine triad proteins superfamily. HINT1 plays an important role in various biological processes, and it has been found in many species. Here, we report the first structure (at a 2.34 Å resolution) of a complex of human HINT1 with a non-hydrolyzable analog of an Ap₄A dinucleotide, containing bis-phosphorothioated glycerol mimicking a polyphosphate chain, obtained from a primitive monoclinic space group P2₁ crystal. In addition, the apo form of hHINT1 at the space group P2₁ refined to 1.92 Å is reported for comparative studies.