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Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 23 Å resolution

P. Kolenko, D. Rozbeský, O. Vaněk, K. Bezouška, J. Hašek, J. Dohnálek

. 2011 ; 67 (Pt 12) : 1519-1523. [pub] 20111130

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc12022072

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.

Citace poskytuje Crossref.org

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