Molecular model of the N-terminal receptor-binding domain of the human CD6 ligand ALCAM. |
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| Authors: | J Bajorath M A Bowen and A Aruffo |
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| Affiliation: | Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121, USA. |
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| Abstract: | CD6-ligand interactions have been implicated in the regulation of T-cell adhesion and activation. CD6 is a member of the scavenger receptor family, whereas its human ligand (ALCAM) belongs to the immunoglobulin superfamily. The extracellular region of ALCAM includes five immunoglobulin-like domains. As a fusion protein, the N-terminal extracellular domain of ALCAM (ALCAMD1) binds specifically to CD6. We report the construction, assessment, and analysis of a molecular model of ALCAMD1. The model defines the CDR-analogous loops, the location of N-linked glycosylation sites, and residues that form the beta-sheet faces of the immunoglobulin-like domain. Predicted structural characteristics of the A'GFCC'C" face of the model are consistent with the presence of monomeric and dimeric forms of ALCAMD1, which has implications for the receptor-ligand interactions. |
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| Keywords: | comparative modeling CD6 ligand immunoglobulin superfamily T-cell functions |
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