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Crystal structure of the human NKR-P1 bound to its lymphocyte ligand LLT1 reveals receptor clusterin...

Crystal structure of the human NKR-P1 bound to its lymphocyte ligand LLT1 reveals receptor clusterin...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2541569116

Crystal structure of the human NKR-P1 bound to its lymphocyte ligand LLT1 reveals receptor clustering in the immune synapse

About this item

Full title

Crystal structure of the human NKR-P1 bound to its lymphocyte ligand LLT1 reveals receptor clustering in the immune synapse

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2021-06

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Human NKR-P1 (CD161, KLRB1) and its ligand LLT1 (CLEC2D) are a prototypical inhibitory C-type lectin-like receptor:ligand pair of NK cells with a critical role in homing lymphocytes to immune-privileged sites, particularly in multiple sclerosis, rheumatoid arthritis, and Crohn's disease. Furthermore, NKR-P1:LLT1 inhibitory signaling is associated w...

Alternative Titles

Full title

Crystal structure of the human NKR-P1 bound to its lymphocyte ligand LLT1 reveals receptor clustering in the immune synapse

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2541569116

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2541569116

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/2021.06.16.448687