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EC Number	Crystallization (Commentary)
2.3.1.43	in complex with antibody 27C3, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.0) and 5% (w/v) PEG 20000
2.3.1.43	molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT

EC Number

Crystallization (Commentary)

2.3.1.43

in complex with antibody 27C3, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.0) and 5% (w/v) PEG 20000

2.3.1.43

molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT

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Release 2023.1 (January 2023)