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The T cell surface glycoprotein, CD6 binds CD166 in the first example of an interaction between a scavenger receptor cysteine-rich domain and an immunoglobulin-like domain. We report that in human these proteins interact with a K D =0.4-1.0 μM and K off ≥0.4-0.63 s -1 , typical of many leukocyte membrane protein interactions. CD166 also interacts in a homophilic manner but with around 100-fold lower affinity (K D =29-48 μM and K off ≥ 5.3 s -1 ). At concentrations, that will block the CD6/CD166 interaction, soluble monomeric CD6 and CD166 inhibit antigen-specific human T cell responses. This is consistent with extracellular engagement between CD6 and CD166 being required for an optimal immune response. © 2004 Wiley-VCH Verlag GmbH & Co. KGaA.

Original publication

DOI

10.1002/eji.200424856

Type

Journal article

Journal

European Journal of Immunology

Publication Date

01/04/2004

Volume

34

Pages

930 - 940