Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 67, Issue -, Pages 1519-1523Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111046203
Keywords
NKR-P1A; merohedral twinning; mutation
Funding
- EC [LSHG-CT-2006-031220]
- ELISA [226716, 09.1.81077, 09.2.90262]
- Czech Science Foundation [305/07/1073, P302/11/0855]
- Academy of Sciences (Praemium Academiae)
- Ministry of Education of the Czech Republic [MSM 21620808, 1M0505]
- Charles University Prague [263209/2011, 403211/2011]
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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 angstrom 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.
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