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Title: Molecular modeling of D151Y and M391T mutations in the LDL receptor
Authors: Nutjaree Jeenduang
Chamras Promptmas
Klai upsorn S Pongrapeeporn
Sureerut Porntadavity
Mahidol University
Heart Genetics Company
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 12-Dec-2008
Citation: Biochemical and Biophysical Research Communications. Vol.377, No.2 (2008), 355-360
Abstract: The low-density lipoprotein receptor (LDLR) is a key regulator of cholesterol homeostasis, and defects in the function of LDLR result in familial hypercholesterolemia (FH). In the present study, we performed structural analyses of two novel LDLR mutations, D151Y and M391T. Both mutations occurred in conserved residues of LDLR. The D151Y mutation, in the ligand binding domain, caused an elimination of a hydrogen bond in the calcium binding site, higher solvent accessibility and a loss of negative charge in the Y151 residue. On the other hand, the M391T mutation, in the β-propeller of the epidermal growth factor (EGF) precursor homology domain, caused an additional hydrogen bond to form, higher solvent accessibility and a distortion of the β-strand. These data suggest that the irregular structures of the mutated LDLRs are likely to cause the functional defect that contributes to the pathology of FH. © 2008 Elsevier Inc. All rights reserved.
ISSN: 10902104
Appears in Collections:Scopus 2006-2010

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