| BMC Evolutionary Biology | |
| The evolution of the class A scavenger receptors | |
| Research Article | |
| G Brian Golding1  Brendan J McConkey2  Fiona J Whelan3  Dawn M E Bowdish3  Conor J Meehan4  | |
| [1] Department of Biology, McMaster University, 1280 Main Street West, L8S 4L8, Hamilton, Ontario, Canada;Department of Biology, University of Waterloo, 200 University Avenue West, N2L 3G1, Waterloo, Ontario, Canada;Department of Pathology and Molecular Medicine, McMaster University, 1200 Main Street West, L8N 3Z5, Hamilton, Ontario, Canada;Faculty of Biochemistry and Molecular Biology, Dalhousie University, 5080 College Street, B3H 4R2, Halifax, Nova Scotia, Canada; | |
| 关键词: Class A scavenger receptor; Innate immunity; Scavenger receptor; Pattern recognition receptor; Scavenger receptor cysteine rich domain; Comparative evolution; | |
| DOI : 10.1186/1471-2148-12-227 | |
| received in 2012-07-06, accepted in 2012-10-31, 发布年份 2012 | |
| 来源: Springer | |
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【 摘 要 】
BackgroundThe class A scavenger receptors are a subclass of a diverse family of proteins defined based on their ability to bind modified lipoproteins. The 5 members of this family are strikingly variable in their protein structure and function, raising the question as to whether it is appropriate to group them as a family based on their ligand binding abilities.ResultsTo investigate these relationships, we defined the domain architecture of each of the 5 members followed by collecting and annotating class A scavenger receptor mRNA and amino acid sequences from publicly available databases. Phylogenetic analyses, sequence alignments, and permutation tests revealed a common evolutionary ancestry of these proteins, indicating that they form a protein family. We postulate that 4 distinct gene duplication events and subsequent domain fusions, internal repeats, and deletions are responsible for the diverse protein structures and functions of this family. Despite variation in domain structure, there are highly conserved regions across all 5 members, indicating the possibility that these regions may represent key conserved functional motifs.ConclusionsWe have shown with significant evidence that the 5 members of the class A scavenger receptors form a protein family. We have indicated that these receptors have a common origin which may provide insight into future functional work with these proteins.
【 授权许可】
Unknown
© Whelan et al.; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO202311109841102ZK.pdf | 1358KB |
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