title: High-resolution X-ray structure of the rabbit histidine triad nucleotide-binding protein 1 (rHINT1)-adenosine complex at 1.10 Å resolution.
abstract: Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch in the histidine-triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the first complete structure of the rabbit HINT1-adenosine complex is reported at 1.10 Å resolution, which is one of the highest resolutions obtained for a HINT1 structure. The final structure has an R(cryst) of 14.25% (R(free) = 16.77%) and the model exhibits good stereochemical qualities. A detailed analysis of the atomic resolution data allowed an update of the details of the protein structure in comparison to previously published data.
authors.affiliation: Department of Bioorganic Chemistry, Centre of Molecular and Macromolecular Studies of the Polish Academy of Sciences, Łódź, Poland. rdolot@cbmm.lodz.pl
authors.forename: Rafał
authors.initials: R
authors.lastname: Dolot
authors.forename: Magdalena
authors.initials: M
authors.lastname: Ozga
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Krakowiak
authors.forename: Barbara
authors.initials: B
authors.lastname: Nawrot
mesh_terms: D000241:Adenosine / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011817:Rabbits; D040681:Structural Homology, Protein
chemical_list: C097552:histidine triad protein; D006867:Hydrolases; D000241:Adenosine