ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Nkrp1 family, from lectins to protein interacting molecules.Molecules (Basel, Switzerland) · 2015Article
- Complexity and Diversity of the NKR-P1:Clr (Klrb1:Clec2) Recognition Systems.Frontiers in immunology · 2014Review
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6 authors.
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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.
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