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Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis

Duan, Jianxin ; Dahlbäck, Björn LU and Villoutreix, Bruno O. (2001) In FEBS Letters 499(1-2). p.127-132
Abstract
Apolipoprotein RI (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein, Sensitive sequence starches, 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.
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Lipocalin, Apolipoprotein M, Comparative modeling, Site-directed mutagenesis
in
FEBS Letters
volume
499
issue
1-2
pages
127 - 132
publisher
Wiley-Blackwell
external identifiers
  • wos:000169549100027
  • scopus:0035875801
ISSN
1873-3468
DOI
10.1016/S0014-5793(01)02544-3
language
English
LU publication?
yes
id
83c71c1f-57ed-4548-b595-998386d457e4 (old id 1119113)
date added to LUP
2016-04-01 16:20:22
date last changed
2025-10-14 11:24:38
@article{83c71c1f-57ed-4548-b595-998386d457e4,
  abstract     = {{Apolipoprotein RI (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein, Sensitive sequence starches, 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.}},
  author       = {{Duan, Jianxin and Dahlbäck, Björn and Villoutreix, Bruno O.}},
  issn         = {{1873-3468}},
  keywords     = {{Lipocalin; Apolipoprotein M; Comparative modeling; Site-directed mutagenesis}},
  language     = {{eng}},
  number       = {{1-2}},
  pages        = {{127--132}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis}},
  url          = {{http://dx.doi.org/10.1016/S0014-5793(01)02544-3}},
  doi          = {{10.1016/S0014-5793(01)02544-3}},
  volume       = {{499}},
  year         = {{2001}},
}