Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis
(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:
https://lup.lub.lu.se/record/1119113
- author
- Duan, Jianxin ; Dahlbäck, Björn LU and Villoutreix, Bruno O.
- organization
- publishing date
- 2001
- 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
- 2022-03-14 23:51:25
@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}}, }