The evolution of the class A scavenger receptors

<p>Abstract</p> <p>Background</p> <p>The 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...

Full description

Bibliographic Details
Main Authors: Whelan Fiona J, Meehan Conor J, Golding G Brian, McConkey Brendan J, E Bowdish Dawn M
Format: Article
Language:English
Published: BMC 2012-11-01
Series:BMC Evolutionary Biology
Subjects:
Online Access:http://www.biomedcentral.com/1471-2148/12/227
id doaj-3d5c95a10587427c98e9394299ce414a
record_format Article
spelling doaj-3d5c95a10587427c98e9394299ce414a2021-09-02T03:01:57ZengBMCBMC Evolutionary Biology1471-21482012-11-0112122710.1186/1471-2148-12-227The evolution of the class A scavenger receptorsWhelan Fiona JMeehan Conor JGolding G BrianMcConkey Brendan JE Bowdish Dawn M<p>Abstract</p> <p>Background</p> <p>The 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.</p> <p>Results</p> <p>To 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.</p> <p>Conclusions</p> <p>We 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.</p> http://www.biomedcentral.com/1471-2148/12/227Class A scavenger receptorInnate immunityScavenger receptorPattern recognition receptorScavenger receptor cysteine rich domainComparative evolution
collection DOAJ
language English
format Article
sources DOAJ
author Whelan Fiona J
Meehan Conor J
Golding G Brian
McConkey Brendan J
E Bowdish Dawn M
spellingShingle Whelan Fiona J
Meehan Conor J
Golding G Brian
McConkey Brendan J
E Bowdish Dawn M
The evolution of the class A scavenger receptors
BMC Evolutionary Biology
Class A scavenger receptor
Innate immunity
Scavenger receptor
Pattern recognition receptor
Scavenger receptor cysteine rich domain
Comparative evolution
author_facet Whelan Fiona J
Meehan Conor J
Golding G Brian
McConkey Brendan J
E Bowdish Dawn M
author_sort Whelan Fiona J
title The evolution of the class A scavenger receptors
title_short The evolution of the class A scavenger receptors
title_full The evolution of the class A scavenger receptors
title_fullStr The evolution of the class A scavenger receptors
title_full_unstemmed The evolution of the class A scavenger receptors
title_sort evolution of the class a scavenger receptors
publisher BMC
series BMC Evolutionary Biology
issn 1471-2148
publishDate 2012-11-01
description <p>Abstract</p> <p>Background</p> <p>The 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.</p> <p>Results</p> <p>To 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.</p> <p>Conclusions</p> <p>We 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.</p>
topic Class A scavenger receptor
Innate immunity
Scavenger receptor
Pattern recognition receptor
Scavenger receptor cysteine rich domain
Comparative evolution
url http://www.biomedcentral.com/1471-2148/12/227
work_keys_str_mv AT whelanfionaj theevolutionoftheclassascavengerreceptors
AT meehanconorj theevolutionoftheclassascavengerreceptors
AT goldinggbrian theevolutionoftheclassascavengerreceptors
AT mcconkeybrendanj theevolutionoftheclassascavengerreceptors
AT ebowdishdawnm theevolutionoftheclassascavengerreceptors
AT whelanfionaj evolutionoftheclassascavengerreceptors
AT meehanconorj evolutionoftheclassascavengerreceptors
AT goldinggbrian evolutionoftheclassascavengerreceptors
AT mcconkeybrendanj evolutionoftheclassascavengerreceptors
AT ebowdishdawnm evolutionoftheclassascavengerreceptors
_version_ 1721181003475582976