CLUSTAL 2.1 multiple sequence alignment of diphospho mevalonate decarboxylases from <i>Brugia malayi</i> (<i>Bm</i>MVD), <i>Loa loa</i> (<i>Ll</i>MVD), <i>Homo sapiens</i> (<i>Hs</i>MVD) and <i>Saccharomyces cerevisiae</i> (<i>Sc</i>MVD), highlighting two regions in the published <i>Bm</i>MVD sequences that diverge from the consensus between the orthologous protein sequences.
Elizabeth Bilsland
Daniel M. Bean
Eileen Devaney
Stephen G. Oliver
10.1371/journal.pntd.0004401.g001
https://plos.figshare.com/articles/figure/_CLUSTAL_2_1_multiple_sequence_alignment_of_diphospho_mevalonate_decarboxylases_from_Brugia_malayi_Bm_MVD_Loa_loa_Ll_MVD_Homo_sapiens_Hs_MVD_and_Saccharomyces_cerevisiae_Sc_MVD_highlighting_two_regions_in_the_published_Bm_MVD_sequences_that_diverge_from_t/1642732
<p>These could be due to the presence of different splice variants of the <i>Brugia</i> enzyme, natural insertions or errors in the published sequence.* conserved residues;: chemically conserved changes;. non-conserved changes.</p>
2016-01-28 12:42:22
World Health Organization
filarial
compound
aid antihelmintic drug development
Brugia malayi drug targets
contracting lymphatic filariasis
complement yeast deletions
Identify Novel Compounds
Brugia malayi BackgroundLymphatic filariasis
strain
parasite enzymes
worms Wuchereria bancrofti
Brugia malayi enzymes