Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2

Hong Cheng; Vered Schwell; Brett R. Curtis; Ruzaliya Fazlieva; Heinrich Roder; Kerry S. Campbell

doi:10.1016/j.str.2019.01.009

Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2

Hong Cheng
, Vered Schwell
, Brett R. Curtis
, Ruzaliya Fazlieva
, Heinrich Roder
, Kerry S. Campbell

Fox Chase Cancer Center

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

KIR3DL1 is an inhibitory receptor that regulates natural killer (NK) cell immune function. Cheng et al. describe NMR-based studies of its disordered cytoplasmic portion. The work characterized conformation dynamics as it binds with SH2 domains of the tyrosine phosphatase, SHP-2, which has broad implications in understanding inhibitory receptor function.

Original language	English
Pages (from-to)	639-650.e2
Journal	Structure
Volume	27
Issue number	4
DOIs	https://doi.org/10.1016/j.str.2019.01.009
State	Published - Apr 2 2019

Keywords

NMR
SH2 domain
SHP-2
immune receptors
immunoreceptor tyrosine-based inhibitory motif (ITIM)
inhibitory receptor
intrinsically disordered protein (IDP)
killer cell Ig-like receptor (KIR)
protein-lipid interaction
tyrosine phosphorylation

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10.1016/j.str.2019.01.009

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title = "Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2",

abstract = "KIR3DL1 is an inhibitory receptor that regulates natural killer (NK) cell immune function. Cheng et al. describe NMR-based studies of its disordered cytoplasmic portion. The work characterized conformation dynamics as it binds with SH2 domains of the tyrosine phosphatase, SHP-2, which has broad implications in understanding inhibitory receptor function.",

keywords = "NMR, SH2 domain, SHP-2, immune receptors, immunoreceptor tyrosine-based inhibitory motif (ITIM), inhibitory receptor, intrinsically disordered protein (IDP), killer cell Ig-like receptor (KIR), protein-lipid interaction, tyrosine phosphorylation",

author = "Hong Cheng and Vered Schwell and Curtis, \{Brett R.\} and Ruzaliya Fazlieva and Heinrich Roder and Campbell, \{Kerry S.\}",

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year = "2019",

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AU - Cheng, Hong

AU - Schwell, Vered

AU - Curtis, Brett R.

AU - Fazlieva, Ruzaliya

AU - Roder, Heinrich

AU - Campbell, Kerry S.

PY - 2019/4/2

Y1 - 2019/4/2

N2 - KIR3DL1 is an inhibitory receptor that regulates natural killer (NK) cell immune function. Cheng et al. describe NMR-based studies of its disordered cytoplasmic portion. The work characterized conformation dynamics as it binds with SH2 domains of the tyrosine phosphatase, SHP-2, which has broad implications in understanding inhibitory receptor function.

AB - KIR3DL1 is an inhibitory receptor that regulates natural killer (NK) cell immune function. Cheng et al. describe NMR-based studies of its disordered cytoplasmic portion. The work characterized conformation dynamics as it binds with SH2 domains of the tyrosine phosphatase, SHP-2, which has broad implications in understanding inhibitory receptor function.

KW - NMR

KW - SH2 domain

KW - SHP-2

KW - immune receptors

KW - immunoreceptor tyrosine-based inhibitory motif (ITIM)

KW - inhibitory receptor

KW - intrinsically disordered protein (IDP)

KW - killer cell Ig-like receptor (KIR)

KW - protein-lipid interaction

KW - tyrosine phosphorylation

UR - https://www.scopus.com/pages/publications/85063342230

U2 - 10.1016/j.str.2019.01.009

DO - 10.1016/j.str.2019.01.009

M3 - Article

C2 - 30773397

AN - SCOPUS:85063342230

SN - 0969-2126

VL - 27

SP - 639-650.e2

JO - Structure

JF - Structure

IS - 4

ER -

Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2

Abstract

Keywords

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