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A robust all-atom model for LCAT generated by homology modeling.

Jere P Segrest1, Martin K Jones1, Andrea Catte1

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|January 16, 2015
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Summary

Researchers developed a novel homology model for human lecithin-cholesterol acyltransferase (LCAT) by combining phospholipase A2 and bacteriophage tubulin structures. This model explains LCAT

Keywords:
apolipoproteinscholesterol/effluxhigh density lipoproteinlecithin:cholesterol acyltransferasephospholipases/A2

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Modeling

Background:

  • Lecithin-cholesterol acyltransferase (LCAT) plays a crucial role in reverse cholesterol transport.
  • LCAT esterifies cholesterol, a key step in removing excess cholesterol from peripheral tissues.
  • Understanding LCAT structure is vital for its antiatherogenic function.

Purpose of the Study:

  • To create a novel homology model for human LCAT.
  • To elucidate the structural basis of LCAT activity and substrate binding.
  • To provide insights into the antiatherogenic role of high-density lipoprotein (HDL).

Main Methods:

  • Homology modeling combining phospholipase A2 (PLA2) and bacteriophage tubulin PhuZ structures.
  • Analysis of structural motifs and their correlation with experimental data.
  • Investigating the catalytic triad and substrate binding site interactions.

Main Results:

  • A novel homology model for human LCAT was successfully generated.
  • The model reveals an extended hydrophobic binding trough and precise positioning of the ester bond near the catalytic nucleophile (S181).
  • Key residues (E149, K128, R147) critical for LCAT activity and specificity were identified in relation to S181.

Conclusions:

  • The novel LCAT model offers a structural explanation for substrate transfer from HDL to the catalytic triad.
  • This model advances the understanding of LCAT's function in reverse cholesterol transport and its antiatherogenic properties.