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.

Significance The function of the T-cell coreceptor CD4 presents a long-standing puzzle. Although it is among the most potent modulators of immune responses, CD4 interacts with its binding partner, peptide-major histocompatibility class II (pMHC II), with previously unmeasurably low affinity. Here, we set a new upper limit for the solution affinity of CD4 and pMHC II and show that the two-dimensional dissociation constant in supported lipid bilayers is as much as two to three orders of magnitude higher than that for other interacting leukocyte surface proteins. These findings extend the known physical limits of functional protein interactions at the cell surface and suggest new ways that T cells may use differential receptor affinities during antigen recognition and discrimination.

Original publication

DOI

10.1073/pnas.1513918113

Type

Journal article

Journal

Proceedings of the National Academy of Sciences

Publisher

Proceedings of the National Academy of Sciences

Publication Date

17/05/2016

Volume

113

Pages

5682 - 5687