Article
Apolipoprotein E;-low density lipoprotein receptor interaction. Influences of basic residue and amphipathic alpha-helix organization in the ligand.
Journal of lipid research - 1 Jul 2000
Zaiou M, Arnold K S, Newhouse Y M, Innerarity T L, Weisgraber K H, Segall M L, Phillips M C, Lund-Katz S
Abstract excerpt
Conserved lysines and arginines within amino acids 140-150 of apolipoprotein (apo) E are crucial for the interaction between apoE and the low density lipoprotein receptor (LDLR). To explore the roles of amphipathic alpha-helix and basic residue organization in the binding process, we performed site-directed mutagenesis on the 22-kDa fragment of apoE (amino acids 1-191). Exchange of lysine and arginine at...
Topics
- Amino Acid Sequence
- Amino Acids, Diamino
- Apolipoproteins E
- Circular Dichroism
- Conserved Sequence
- Escherichia coli
- Humans
- Ligands
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Binding