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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2e2f5009dd934a8381838529885caa65
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id	oai:doaj.org-article:2e2f5009dd934a8381838529885caa65
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spelling	oai:doaj.org-article:2e2f5009dd934a8381838529885caa652021-12-02T14:25:17ZStructural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C10.1038/s41467-021-22359-x2041-1723https://doaj.org/article/2e2f5009dd934a8381838529885caa652021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22359-xhttps://doaj.org/toc/2041-1723KIR2DL2 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.Shoeib MoradiSanda StankovicGeraldine M. O’ConnorPhillip PymmBruce J. MacLachlanCamilla FaoroChristelle RetièreLucy C. SullivanPhilippa M. SaundersJacqueline WidjajaShea Cox-LivingstoneJamie RossjohnAndrew G. BrooksJulian P. VivianNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
description	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.
format	article
author	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
author_facet	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
author_sort	Shoeib Moradi
title	Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
title_short	Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
title_full	Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
title_fullStr	Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
title_full_unstemmed	Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C
title_sort	structural plasticity of kir2dl2 and kir2dl3 enables altered docking geometries atop hla-c
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2e2f5009dd934a8381838529885caa65
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Structural plasticity of KIR2DL2 and KIR2DL3 enables altered docking geometries atop HLA-C

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