1kjc

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL OF THE HUMAN CD6 LIGAND ALCAM (ACTIVATED LEUKOCYTE-CELL ADHESION MOLECULE), N-TERMINAL RECEPTOR- BINDING DOMAIN

spinqualitylabelsall models 1kjc Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed 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. Molecular model of the N-terminal receptor-binding domain of the human CD6 ligand ALCAM.,Bajorath J, Bowen MA, Aruffo A Protein Sci. 1995 Aug;4(8):1644-7. PMID:8520490 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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