Structural highlights
Function
[KLRBA_MOUSE] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.[1]
Publication Abstract from PubMed
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 A 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.
Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 A resolution.,Kolenko P, Rozbesky D, Vanek O, Bezouska K, Hasek J, Dohnalek J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1519-23., Epub 2011 Nov 30. PMID:22139156[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carlyle JR, Mesci A, Ljutic B, Belanger S, Tai LH, Rousselle E, Troke AD, Proteau MF, Makrigiannis AP. Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of mouse NK cells. J Immunol. 2006 Jun 15;176(12):7511-24. PMID:16751398
- ↑ Kolenko P, Rozbesky D, Vanek O, Bezouska K, Hasek J, Dohnalek J. Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1519-23., Epub 2011 Nov 30. PMID:22139156 doi:10.1107/S1744309111046203
