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Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 A 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.

SUBMITTER: Kolenko P 

PROVIDER: S-EPMC3232129 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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

Kolenko Petr P   Rozbeský Daniel D   Vaněk Ondřej O   Bezouška Karel K   Hašek Jindřich J   Dohnálek Jan J  

Acta crystallographica. Section F, Structural biology and crystallization communications 20111130 Pt 12

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  ...[more]

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