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

Publication date: June 2016
Source:International Journal of Biological Macromolecules, Volume 87
Author(s): Rafał Dolot, Renata Kaczmarek, Aleksandra Sęda, Agnieszka Krakowiak, Janina Baraniak, Barbara Nawrot
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 2.34Å 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 1.92Å is reported for comparative studies.

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