A novel mutation in the ligand binding domain of the low-density lipoprotein receptor gene in a Syrian family

This LDLR mutation in exon 4 constitutes a cysteine substitution. The cysteine of codon 163 is the last aminoacid of the IV repeat region of the ligand binding domain of the LDL receptor. and is a highly conserved residue. This allows us to speculate that this mutation produces an allele that interferes with the binding of the ligand to the receptor ( Class 3 Phenotype). However, this mutation may also have an effect on the transport of the protein between the endoplasmatic reticulum and the Golgi apparatus producing a class 2 Phenotype. The fact that this transition occurs in a highly conserved residue contributes to our belief that it is a disease-causing sequence variant. In the same family we were able to identify another novel single aminoacid substitution (C255Y) in exon 6 of the LDL receptor gene.

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