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.

Institute of Macromolecular Chemistry AS CR vvi Prague Czech Republic

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Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

Nkrp1 family, from lectins to protein interacting molecules

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PDB
3T3A