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

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

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 autho...

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Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2021-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-22359-x

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