Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution

0369318 - ÚMCH 2012 RIV GB eng J - Journal Article
Kolenko, Petr - Rozbeský, Daniel - Vaněk, Ondřej - Bezouška, Karel - Hašek, Jindřich - Dohnálek, Jan
Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. Roč. 67, č. 12 (2011), s. 1519-1523. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA ČR GA305/07/1073; GA ČR GAP302/11/0855; GA MŠMT 1M0505
Institutional research plan: CEZ:AV0Z40500505; CEZ:AV0Z50200510; CEZ:AV0Z10100521
Keywords : NKR-P1A * merohedral twinning * mutation
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 0.506, year: 2011

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 A° resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 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.
Permanent Link: http://hdl.handle.net/11104/0203413