About: Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties     Goto   Sponge   NotDistinct   Permalink

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Description
  • Interactions between C-type lectin-like NK cell receptors and their protein ligands form one of the key recognition mechanisms of the innate immune system that is involved in the elimination of cells that have been malignantly transformed, virally infected, or stressed by chemotherapy or other factors. We determined an x-ray structure for the extracellular domain of mouse C-type lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F. Clr-g forms dimers in the crystal structure resembling those of human CD69. This newly reported structure, together with the previously determined structure of mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic profiles for other closely related receptors and ligands. Despite the high similarity among Clr-g, Clr-b, and human CD69, these molecules have fundamentally different electrostatics, with distinct polarization of Clr-g. The electrostatic profile of NKR-P1F is complementary to that of Clr-g, which suggests a plausible interaction mechanism based on contacts between surface sites of opposite potential.
  • Interactions between C-type lectin-like NK cell receptors and their protein ligands form one of the key recognition mechanisms of the innate immune system that is involved in the elimination of cells that have been malignantly transformed, virally infected, or stressed by chemotherapy or other factors. We determined an x-ray structure for the extracellular domain of mouse C-type lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F. Clr-g forms dimers in the crystal structure resembling those of human CD69. This newly reported structure, together with the previously determined structure of mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic profiles for other closely related receptors and ligands. Despite the high similarity among Clr-g, Clr-b, and human CD69, these molecules have fundamentally different electrostatics, with distinct polarization of Clr-g. The electrostatic profile of NKR-P1F is complementary to that of Clr-g, which suggests a plausible interaction mechanism based on contacts between surface sites of opposite potential. (en)
Title
  • Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties
  • Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties (en)
skos:prefLabel
  • Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties
  • Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties (en)
skos:notation
  • RIV/00216208:11310/12:10126859!RIV13-GA0-11310___
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(EE2.3.30.0029), P(GA303/09/0477), P(GA305/07/1073), P(GAP207/10/1040), P(GAP302/11/0855), P(GD305/09/H008), P(KJB101120805), S, Z(AV0Z40500505), Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika
  • 10
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 151959
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/12:10126859
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • refinement; sensitivity; rat; CD69; mice; family; macromolecular crystallography; natural-killer-cells; missing-self-recognition; C-type lectin (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [4CC8F4D6733B]
http://linked.open...i/riv/nazevZdroje
  • Journal of Immunology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 189
http://linked.open...iv/tvurceVysledku
  • Bezouška, Karel
  • Dohnálek, Jan
  • Dušková, Jarmila
  • Hašek, Jindřich
  • Man, Petr
  • Novák, Petr
  • Skálová, Tereza
  • Vaněk, Ondřej
  • Kolenko, Petr
  • Hanč, Pavel
  • Kotýnková, Kristýna
  • Koval, Tomáš
http://linked.open...ain/vavai/riv/wos
  • 000310710600022
http://linked.open...n/vavai/riv/zamer
issn
  • 0022-1767
number of pages
http://bibframe.org/vocab/doi
  • 10.4049/jimmunol.1200880
http://localhost/t...ganizacniJednotka
  • 11310
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