Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C

Shoeib Moradi; Sanda Stankovic; Geraldine M. O’Connor; Phillip Pymm; Bruce J. MacLachlan; Camilla Faoro; Christelle Retière; Lucy C. Sullivan; Philippa M. Saunders; Jacqueline Widjaja; Shea Cox-Livingstone; Jamie Rossjohn; Andrew G. Brooks; Julian P. Vivian

doi:10.1038/s41467-021-22359-x

Nature Communications (Apr 2021)

Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C

Shoeib Moradi,
Sanda Stankovic,
Geraldine M. O’Connor,
Phillip Pymm,
Bruce J. MacLachlan,
Camilla Faoro,
Christelle Retière,
Lucy C. Sullivan,
Philippa M. Saunders,
Jacqueline Widjaja,
Shea Cox-Livingstone,
Jamie Rossjohn,
Andrew G. Brooks,
Julian P. Vivian

Affiliations

Shoeib Moradi: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University
Sanda Stankovic: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Geraldine M. O’Connor: School of Medicine, University of Central Lancashire
Phillip Pymm: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University
Bruce J. MacLachlan: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University
Camilla Faoro: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University
Christelle Retière: Etablissement Français du Sang, Nantes
Lucy C. Sullivan: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Philippa M. Saunders: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Jacqueline Widjaja: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Shea Cox-Livingstone: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Jamie Rossjohn: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University
Andrew G. Brooks: Department of Microbiology and Immunology, Peter Doherty Institute for Infection and Immunity, The University of Melbourne
Julian P. Vivian: Infection and Immunity Program and Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University

DOI: https://doi.org/10.1038/s41467-021-22359-x
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 11

Abstract

Read online

KIR2DL2 and KIR2DL3 are two inhibitory members of the killer-cell immunoglobulin-like receptors (KIR) family that share a common HLA-I preference in binding HLA from the C1 group. However, it is still unclear to what extent binding and function is equivalent between KIR2DL2 and 2DL3. Here, the authors present the crystal structures of KIR2DL2 and 2DL3 in complex with HLA-C*07:02 and observe differences in HLA-C recognition between KIR2DL2 and 2DL3, which correlates with differences in HLA-C binding preference as they show with mutagenesis and binding studies.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal