A Systematic Study on Structure and Function of ATPase of Wuchereria bancrofti
Identifieur interne : 002E42 ( Main/Exploration ); précédent : 002E41; suivant : 002E43A Systematic Study on Structure and Function of ATPase of Wuchereria bancrofti
Auteurs : Md. Saiful Islam [Bangladesh] ; Noman Ibna Amin Patwary [Bangladesh] ; Nazmul Hasan Muzahid [Bangladesh] ; Shah Md. Shahik [Bangladesh] ; Md. Sohel [Bangladesh] ; Md. Anayet Hasan [Bangladesh]Source :
- Toxicology International [ 0971-6580 ] ; 2014.
Abstract
Analyzing the structures and functions of different proteins of
In this study we worked on the protein ATPase of Wuchereria bancrofti which has been annotated from National Center for Biotechnology Information (NCBI). Various computational tools and databases have been used to determine the various characteristics of that enzyme such as physiochemical properties, secondary structure, three-dimensional (3D) structure, conserved domain, epitope, and their molecular evolutionary relationship.
Subcellular localization of ATPase was identified and we have found that 55.5% are localized in the cytoplasm. Secondary and 3D structure of this protein was also predicted. Both structure and function analysis of ATPase of Wuchereria bancrofti showed unique nonhomologous epitope sites and nonhomologous antigenicity sites. Moreover, it resulted in 15 ligand drug-binding sites in its tertiary structure.
Structure prediction of these proteins and detection of binding sites and antigenicity sites from this study would indicate a potential target aiding docking studies for therapeutic designing against filariasis.
Url:
DOI: 10.4103/0971-6580.155357
PubMed: 25948965
PubMed Central: 4413409
Affiliations:
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Le document en format XML
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<series><title level="j">Toxicology International</title>
<idno type="ISSN">0971-6580</idno>
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<imprint><date when="2014">2014</date>
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<front><div type="abstract" xml:lang="en"><sec id="st1"><title>Background:</title>
<p>Analyzing the structures and functions of different proteins of <italic>Wuchereria bancrofti</italic>
is very important because till date no effective drug or vaccine has been discovered to treat lymphatic filariasis (LF). ATPase is one of the most important proteins of <italic>Wuchereria bancrofti</italic>
. Adenosine triphosphate (ATP) converts into adenosine diphosphate (ADP) and a free phosphate ion by the action of these ATPase enzymes. Energy releases from these dephosphorylation reactions drive the other chemical reactions in the cell.</p>
</sec>
<sec id="st2"><title>Materials and Methods:</title>
<p>In this study we worked on the protein ATPase of Wuchereria bancrofti which has been annotated from National Center for Biotechnology Information (NCBI). Various computational tools and databases have been used to determine the various characteristics of that enzyme such as physiochemical properties, secondary structure, three-dimensional (3D) structure, conserved domain, epitope, and their molecular evolutionary relationship.</p>
</sec>
<sec id="st3"><title>Result:</title>
<p>Subcellular localization of ATPase was identified and we have found that 55.5% are localized in the cytoplasm. Secondary and 3D structure of this protein was also predicted. Both structure and function analysis of ATPase of Wuchereria bancrofti showed unique nonhomologous epitope sites and nonhomologous antigenicity sites. Moreover, it resulted in 15 ligand drug-binding sites in its tertiary structure.</p>
</sec>
<sec id="st4"><title>Conclusion:</title>
<p>Structure prediction of these proteins and detection of binding sites and antigenicity sites from this study would indicate a potential target aiding docking studies for therapeutic designing against filariasis.</p>
</sec>
</div>
</front>
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<author><name sortKey="Li, N" uniqKey="Li N">N Li</name>
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<affiliations><list><country><li>Bangladesh</li>
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<tree><country name="Bangladesh"><noRegion><name sortKey="Islam, Md Saiful" sort="Islam, Md Saiful" uniqKey="Islam M" first="Md. Saiful" last="Islam">Md. Saiful Islam</name>
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