Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Invariant Vγ9Vδ2 T cells respond to "phosphoantigen" metabolites through binding to the B30.2 domain of butyrophilin BTN3A. Yang et al. (2019) use molecular dynamic simulations based on X-ray structures of distinct B30.2 domain dimers to identify the asymmetric dimer as most active, which has implications for the inside-out signaling mechanism.

Original publication

DOI

10.1016/j.immuni.2019.03.015

Type

Journal article

Journal

Immunity

Publication Date

04/2019

Volume

50

Pages

1026 - 1028

Addresses

Kennedy Institute of Rheumatology, University of Oxford, Oxford, UK. Electronic address: michael.dustin@kennedy.ox.ac.uk.

Keywords

T-Lymphocytes, Antigens, CD, Lymphocyte Activation, X-Rays, Butyrophilins