The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains
<p>Abstract</p> <p>Background</p> <p>Identification and characterization of novel <it>Plasmodium </it>gene families is necessary for developing new anti-malarial therapeutics. The products of the <it>Plasmodium falciparum </it>gene, <it>MB2...
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doaj-082aa6a7d21241bb8795fbf48b95ab302020-11-25T02:30:07ZengBMCBMC Bioinformatics1471-21052004-06-01518310.1186/1471-2105-5-83The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domainsOgunjumo OluwasanmiDeville BenoitNguyen Thanh VRomero Lisa CJames Anthony A<p>Abstract</p> <p>Background</p> <p>Identification and characterization of novel <it>Plasmodium </it>gene families is necessary for developing new anti-malarial therapeutics. The products of the <it>Plasmodium falciparum </it>gene, <it>MB2</it>, were shown previously to have a stage-specific pattern of subcellular localization and proteolytic processing.</p> <p>Results</p> <p>Genes homologous to <it>MB2 </it>were identified in five additional parasite species, <it>P. knowlesi</it>, <it>P. gallinaceum</it>, <it>P. berghei</it>, <it>P. yoelii</it>, and <it>P. chabaudi</it>. Sequence comparisons among the <it>MB2 </it>gene products reveal amino acid conservation of structural features, including putative S1 and GTP-binding domains, and putative signal peptides and nuclear localization signals.</p> <p>Conclusions</p> <p>The combination of domains is unique to this gene family and indicates that <it>MB2 </it>genes comprise a novel family and therefore may be a good target for drug development.</p> http://www.biomedcentral.com/1471-2105/5/83 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ogunjumo Oluwasanmi Deville Benoit Nguyen Thanh V Romero Lisa C James Anthony A |
spellingShingle |
Ogunjumo Oluwasanmi Deville Benoit Nguyen Thanh V Romero Lisa C James Anthony A The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains BMC Bioinformatics |
author_facet |
Ogunjumo Oluwasanmi Deville Benoit Nguyen Thanh V Romero Lisa C James Anthony A |
author_sort |
Ogunjumo Oluwasanmi |
title |
The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains |
title_short |
The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains |
title_full |
The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains |
title_fullStr |
The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains |
title_full_unstemmed |
The <it>MB2 </it>gene family of <it>Plasmodium </it>species has a unique combination of S1 and GTP-binding domains |
title_sort |
<it>mb2 </it>gene family of <it>plasmodium </it>species has a unique combination of s1 and gtp-binding domains |
publisher |
BMC |
series |
BMC Bioinformatics |
issn |
1471-2105 |
publishDate |
2004-06-01 |
description |
<p>Abstract</p> <p>Background</p> <p>Identification and characterization of novel <it>Plasmodium </it>gene families is necessary for developing new anti-malarial therapeutics. The products of the <it>Plasmodium falciparum </it>gene, <it>MB2</it>, were shown previously to have a stage-specific pattern of subcellular localization and proteolytic processing.</p> <p>Results</p> <p>Genes homologous to <it>MB2 </it>were identified in five additional parasite species, <it>P. knowlesi</it>, <it>P. gallinaceum</it>, <it>P. berghei</it>, <it>P. yoelii</it>, and <it>P. chabaudi</it>. Sequence comparisons among the <it>MB2 </it>gene products reveal amino acid conservation of structural features, including putative S1 and GTP-binding domains, and putative signal peptides and nuclear localization signals.</p> <p>Conclusions</p> <p>The combination of domains is unique to this gene family and indicates that <it>MB2 </it>genes comprise a novel family and therefore may be a good target for drug development.</p> |
url |
http://www.biomedcentral.com/1471-2105/5/83 |
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