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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.
Please use this url to cite or link to this publication:
author
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
2008-06-26 13:33:20
date last changed
2018-05-29 10:24:28
@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},
  keyword      = {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},
  volume       = {499},
  year         = {2001},
}