ArticleJournal of molecular modeling2011
Structural analysis of natural killer cell receptor protein 1 (NKR-P1) extracellular domains suggests a conserved long loop region involved in ligand specificity.
Article in Journal of molecular modeling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- NKR-P1A/CD161: A Multifunctional Immune Receptor at the Crossroads of Antitumor Immunity.Biomolecules · 2026Review
- Translational Insights into NK Immunophenotyping: Comparative Surface Marker Analysis and Circulating Immune Cell Profiling in Cancer Immunotherapy.International journal of molecular sciences · 2025Review
- The diverse roles of C-type lectin-like receptors in immunity.Frontiers in immunology · 2023Review
- Protective Vaccination Reshapes Hepatic Response to Blood-Stage Malaria of Genes Preferentially Expressed by NK Cells.Vaccines · 2020Article
- Production of recombinant soluble dimeric C-type lectin-like receptors of rat natural killer cells.Scientific reports · 2019Article
- Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Nkrp1 family, from lectins to protein interacting molecules.Molecules (Basel, Switzerland) · 2015Article
- The c.503T>C Polymorphism in the Human KLRB1 Gene Alters Ligand Binding and Inhibitory Potential of CD161 Molecules.PloS one · 2015Article
- Complexity and Diversity of the NKR-P1:Clr (Klrb1:Clec2) Recognition Systems.Frontiers in immunology · 2014Review
- Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Analysis of the mouse 129-strain Nkrp1-Clr gene cluster reveals conservation of genomic organization and functional receptor-ligand interactions despite significant allelic polymorphism.Immunogenetics · 2011Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Receptor proteins at the cell surface regulate the ability of natural killer cells to recognize and kill a variety of aberrant target cells. The structural features determining the function of natural killer receptor proteins 1 (NKR-P1s) are largely unknown. In the present work, refined homology models are generated for the C-type lectin-like extracellular domains of rat NKR-P1A and NKR-P1B, mouse NKR-P1A, NKR-P1C, NKR-P1F, and NKR-P1G, and human NKR-P1 receptors. Experimental data on secondary structure, tertiary interactions, and thermal transitions are acquired for four of the proteins using Raman and infrared spectroscopy. The experimental and modeling results are in agreement with respect to the overall structures of the NKR-P1 receptor domains, while suggesting functionally significant local differences among species and isoforms. Two sequence regions that are conserved in all analyzed NKR-P1 receptors do not correspond to conserved structural elements as might be expected, but are represented by loop regions, one of which is arranged differently in the constructed models. This region displays high flexibility but is anchored by conserved sequences, suggesting that its position relative to the rest of the domain might be variable. This loop may contribute to ligand-binding specificity via a coupled conformational transition.
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Registered trials
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