title: Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution.
abstract: The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR-P1A has been determined by X-ray diffraction at 2.3 Å resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4(1)22 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I4(1) with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.
authors.affiliation: Institute of Macromolecular Chemistry AS CR, vvi, Prague, Czech Republic. kolenko@imc.cas.cz
authors.forename: Petr
authors.initials: P
authors.lastname: Kolenko
authors.forename: Daniel
authors.initials: D
authors.lastname: Rozbeský
authors.forename: Ondřej
authors.initials: O
authors.lastname: Vaněk
authors.forename: Karel
authors.initials: K
authors.lastname: Bezouška
authors.forename: Jindřich
authors.initials: J
authors.lastname: Hašek
authors.forename: Jan
authors.initials: J
authors.lastname: Dohnálek
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D005110:Extracellular Space / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D009154:Mutation; D055651:NK Cell Lectin-Like Receptor Subfamily B / Q000737:chemistry* / Q000235:genetics; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D055651:NK Cell Lectin-Like Receptor Subfamily B