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...
Main Authors: | , , , , |
---|---|
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 |