Structural highlights
Function
HINT1_HUMAN Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity).
Publication Abstract from PubMed
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 2.34A 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 1.92A is reported for comparative studies.
Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of ApA.,Dolot R, Kaczmarek R, Seda A, Krakowiak A, Baraniak J, Nawrot B Int J Biol Macromol. 2016 Feb 18;87:62-69. doi: 10.1016/j.ijbiomac.2016.02.047. PMID:26905466[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dolot R, Kaczmarek R, Seda A, Krakowiak A, Baraniak J, Nawrot B. Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of ApA. Int J Biol Macromol. 2016 Feb 18;87:62-69. doi: 10.1016/j.ijbiomac.2016.02.047. PMID:26905466 doi:http://dx.doi.org/10.1016/j.ijbiomac.2016.02.047
