Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
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Duan J, Dahlback B, Villoutreix BO
Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
FEBS Lett. 2001 Jun 15;499(1-2):127-32.
- PubMed ID
- 11418126 [ View in PubMed]
- Abstract
Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein. Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family. In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation. Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed. ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.