About: Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution     Goto   Sponge   NotDistinct   Permalink

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  • 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 I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 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.
  • 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 I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 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. (en)
Title
  • Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution
  • Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution (en)
skos:prefLabel
  • Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution
  • Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution (en)
skos:notation
  • RIV/68378271:_____/11:00369318!RIV12-AV0-68378271
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0505), P(GA305/07/1073), P(GAP302/11/0855), S, Z(AV0Z10100521), Z(AV0Z40500505), Z(AV0Z50200510), Z(MSM0021620808)
http://linked.open...iv/cisloPeriodika
  • 12
http://linked.open...vai/riv/dodaniDat
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  • 232815
http://linked.open...ai/riv/idVysledku
  • RIV/68378271:_____/11:00369318
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • NKR-P1A; merohedral twinning; mutation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [816DD745F2B6]
http://linked.open...i/riv/nazevZdroje
  • Acta Crystallographica Section F
http://linked.open...in/vavai/riv/obor
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http://linked.open...vavai/riv/projekt
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http://linked.open...v/svazekPeriodika
  • 67
http://linked.open...iv/tvurceVysledku
  • Bezouška, Karel
  • Dohnálek, Jan
  • Hašek, Jindřich
  • Vaněk, Ondřej
  • Rozbeský, Daniel
  • Kolenko, Petr
http://linked.open...ain/vavai/riv/wos
  • 000297741100011
http://linked.open...n/vavai/riv/zamer
issn
  • 1744-3091
number of pages
http://bibframe.org/vocab/doi
  • 10.1107/S1744309111046203
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