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.

Lymphocyte function associated antigen 1 (LFA-1) is a heterodimer, composed of an αL-chain and a β2-chain. The I-domain is inserted in the ctL-chain and contains a binding site for ICAM-1. To study the adhesive interaction between the I-domain and ICAM-I, we constructed a GPIanchored form of the I-domain and expressed it stabily in BHK-cells. In contrast to the whole LFA-1 molecule (Kd=8nM), no interaction between soluble ICAM-1 dimers and I-domain expressing cells could be detected, suggesting that the ICAM-1/I-domain interaction is of low affinity (Kd>33|

Type

Journal article

Publication Date

1996-12-01T00:00:00+00:00

Volume

10