[HTML][HTML] Sequence conservation of apolipoprotein AI affords novel insights into HDL structure-function
D Bashtovyy, MK Jones, GM Anantharamaiah… - Journal of lipid …, 2011 - ASBMB
We performed alignment of apolipoprotein AI (apoA-I) sequences from 31 species of
animals. We found there is specific conservation of salt bridge-forming residues in the first
30 residues of apoA-I and general conservation of a variety of residue types in the central
domain, helix 2/3 to helix 7/8. In the lipid-associating domain, helix 7 and helix 10 are the
most and least conserved helixes, respectively. Furthermore, eight residues are completely
conserved: P66, R83, P121, E191, and P220, and three of seven Tyr residues in human …
animals. We found there is specific conservation of salt bridge-forming residues in the first
30 residues of apoA-I and general conservation of a variety of residue types in the central
domain, helix 2/3 to helix 7/8. In the lipid-associating domain, helix 7 and helix 10 are the
most and least conserved helixes, respectively. Furthermore, eight residues are completely
conserved: P66, R83, P121, E191, and P220, and three of seven Tyr residues in human …