[HTML][HTML] Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase
AP Beigneux, P Gin, BSJ Davies, MM Weinstein… - Journal of biological …, 2009 - ASBMB
GPIHBP1, a glycosylphosphatidylinositol-anchored endothelial cell protein of the
lymphocyte antigen 6 (Ly6) family, binds lipoprotein lipase (LPL) avidly and is required for
the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 contains two key structural
motifs, an acidic domain and an Ly6 motif (a three-fingered domain specified by 10
cysteines). The acidic domain is required for LPL binding, but the importance of the Ly6
domain is less clear. To explore that issue, we transfected cells with a wild-type GPIHBP1 …
lymphocyte antigen 6 (Ly6) family, binds lipoprotein lipase (LPL) avidly and is required for
the lipolytic processing of triglyceride-rich lipoproteins. GPIHBP1 contains two key structural
motifs, an acidic domain and an Ly6 motif (a three-fingered domain specified by 10
cysteines). The acidic domain is required for LPL binding, but the importance of the Ly6
domain is less clear. To explore that issue, we transfected cells with a wild-type GPIHBP1 …