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

Systematic mutation and thermodynamic analysis of central tyrosine pairs in polyspecific NKG2D receptor interactions.

Molecular immunology - 1 Jan 2011

Culpepper David J, Maddox Michael K, Caldwell Andrew B, McFarland Benjamin J

Abstract excerpt

The homodimeric, activating natural killer cell receptor NKG2D interacts with multiple monomeric ligands polyspecifically, yet without central conformational flexibility. Crystal structures of multiple NKG2D-ligand interactions have identified the NKG2D tyrosine pair Tyr 152 and Tyr 199 as formin...

Read the complete abstract on PubMed

Topics

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

Share to Histocompatibility Antigens Class I
Share to Hydrophobic and Hydrophilic Interactions
Share to Ligands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to NK Cell Lectin-Like Receptor Subfamily K

Share to Solvents

Share to Thermodynamics

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 21074271
DOI: 10.1016/j.molimm.2010.10.007
PMCID: PMC3014408

Genes

MICA
MICB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21074271-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Systematic mutation and thermodynamic analysis of central tyrosine pairs in polyspecific NKG2D receptor interactions.PMID 21074271Read ↗

Combining different design strategies for rational affinity maturation of the MICA-NKG2D interface.Semantic proximity Read ↗

Hydrophobic core evolution of major histocompatibility complex class I chain-related protein A for dramatic enhancing binding affinity.Semantic proximity Read ↗

The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.Semantic proximity Read ↗

Structural studies of allelic diversity of the MHC class I homolog MIC-B, a stress-inducible ligand for the activating immunoreceptor NKG2D.Semantic proximity Read ↗

Conformational Plasticity Revealed by the Cocrystal Structure of NKG2D and Its Class I MHC-like Ligand ULBP3Semantic proximity Read ↗

Elucidation of the molecular interactions that enable stable assembly and structural diversity in multicomponent immune receptors.Semantic proximity Read ↗

Deep mutational scanning reveals transmembrane features governing surface expression of the B cell antigen receptor.Semantic proximity Read ↗

Structure of the HCMV UL16-MICB Complex Elucidates Select Binding of a Viral Immunoevasin to Diverse NKG2D LigandsSemantic proximity Read ↗

Battling BTK mutants with noncovalent inhibitors that overcome Cys481 and Thr474 mutations in Waldenström macroglobulinemia therapy: structural mechanistic insights on the role of fenebrutinib.Semantic proximity Read ↗

Effects of mutations on MUC1-C/ED protein stability and antibody Binding: Structural insight.Semantic proximity Read ↗

Mapping Interaction Sites on Human Chemokine Receptors by Deep Mutational Scanning.Semantic proximity Read ↗

High Affinity Antigen Recognition of the Dual Specific Variants of Herceptin Is Entropy-Driven in Spite of Structural PlasticitySemantic proximity Read ↗

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