Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutation at positively selected positions in the binding site for HLA-C shows that KIR2DL1 is a more refined but less adaptable NK cell receptor than KIR2DL3.

Journal of immunology (Baltimore, Md. : 1950) - 1 Aug 2012

Hilton Hugo G, Vago Luca, Older Aguilar Anastazia M, Moesta Achim K, Graef Thorsten, Abi-Rached Laurent, Norman Paul J, Guethlein Lisbeth A, Fleischhauer Katharina, Parham Peter

Abstract excerpt

Through recognition of HLA class I, killer cell Ig-like receptors (KIR) modulate NK cell functions in human immunity and reproduction. Although a minority of HLA-A and -B allotypes are KIR ligands, HLA-C allotypes dominate this regulation, because they all carry either the C1 epitope recognized b...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to HLA-C Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Killer Cells, Natural

Share to Point Mutation

Share to Protein Binding

Share to Protein Structure, Tertiary

Share to Receptors, KIR2DL1

Share to Receptors, KIR2DL3

Source

Open in PubMed Open full text

Identifiers

PMID: 22772445
DOI: 10.4049/jimmunol.1100431
PMCID: PMC3439511

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22772445-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation at positively selected positions in the binding site for HLA-C shows that KIR2DL1 is a more refined but less adaptable NK cell receptor than KIR2DL3.PMID 22772445Read ↗

Synergistic polymorphism at two positions distal to the ligand-binding site makes KIR2DL2 a stronger receptor for HLA-C than KIR2DL3.Semantic proximity Read ↗

Polymorphic HLA-C Receptors Balance the Functional Characteristics of KIR Haplotypes.Semantic proximity Read ↗

Resurrecting KIR2DP1: A Key Intermediate in the Evolution of Human Inhibitory NK Cell Receptors That Recognize HLA-C.Semantic proximity Read ↗

Allelic variation in KIR2DL3 generates a KIR2DL2-like receptor with increased binding to its HLA-C ligand.Semantic proximity Read ↗

Large spectrum of HLA-C recognition by killer Ig-like receptor (KIR)2DL2 and KIR2DL3 and restricted C1 SPECIFICITY of KIR2DS2: dominant impact of KIR2DL2/KIR2DS2 on KIR2D NK cell repertoire formation.Semantic proximity Read ↗

KIR2DS4 is a product of gene conversion with KIR3DL2 that introduced specificity for HLA-A*11 while diminishing avidity for HLA-C.Semantic proximity Read ↗

Canonical and cross-reactive binding of NK cell inhibitory receptors to HLA-C allotypes is dictated by peptides bound to HLA-CSemantic proximity Read ↗

Natural variation at position 45 in the D1 domain of lineage III killer cell immunoglobulin-like receptors (KIR) has major effects on the avidity and specificity for MHC class I.Semantic proximity Read ↗

The influence of HLA-C and KIR on natural killer cell functionSemantic proximity Read ↗

Innate receptors with high specificity for HLA class I–peptide complexesSemantic proximity Read ↗

Mutational and structural analysis of KIR3DL1 reveals a lineage-defining allotypic dimorphism that impacts both HLA and peptide sensitivity.Semantic proximity Read ↗

Single Nucleotide Polymorphism in KIR2DL1 Is Associated With HLA-C Expression in Global Populations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.