{"id":2,"date":"2012-04-17T16:49:57","date_gmt":"2012-04-17T16:49:57","guid":{"rendered":"https:\/\/protsci-us2b.univ-nantes.fr\/mobpdb\/?page_id=2"},"modified":"2025-02-18T17:55:09","modified_gmt":"2025-02-18T16:55:09","slug":"sample-page","status":"publish","type":"page","link":"https:\/\/protsci-us2b.univ-nantes.fr\/mobpdb\/","title":{"rendered":"Home"},"content":{"rendered":"
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\"Insect<\/a><\/figure>\n<\/div>\n\n\n

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Mosquitoes & moths OBP database (mOBPdb)<\/span><\/strong><\/h2>\n\n\n\n

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Welcome to the database for odorant binding proteins (OBPs) from mosquitoes and moths.<\/strong><\/p>\n\n\n\n

The molecular basis of the odorant perception of mosquitoes and moths is encoded by a series of proteins. One of the members considered very important in this process are the odorant binding proteins (OBPs) which are believed to aid in the transport of odorants and pheromones to the odorant receptors (ORs) and have emerged as novel targets for repellants.<\/p>\n\n\n\n

We are here reporting a manually curated database of OBPs for mosquitoes and moths.<\/p>\n\n\n\n

Among the mosquito OBPs, we report 69 OBPs in Anopheles gambiae<\/em><\/a>, 111 OBPs in the Aedes aegypti <\/em><\/a>and 109 OBPs in the Culex quinquefasciatus<\/em><\/a> genomes [1]. We also report OBPs from other species of the Anopheles<\/a> genus: A. albimanus<\/em><\/a>, A. arabiensis<\/em><\/a>, A. atroparvus<\/em><\/a>, A. christyi<\/em><\/a>, A. coluzzii<\/em><\/a>, A. culicifacies<\/em> A<\/a>, A. darlingi<\/em><\/a>, A. dirus<\/em><\/a>, A. epiroticus<\/em><\/a>, A. funestus<\/em><\/a>, A. maculatus<\/em><\/a>, A. melas<\/em><\/a>, A. merus<\/em><\/a>, A. minimus<\/em><\/a>, A. quadriannulatus<\/em><\/a>, A. sinensis<\/em><\/a>, A. stephensi<\/em><\/a>.<\/p>\n\n\n\n

We are currently adding OBPs from three moths species: Bombyx mori<\/em><\/a>, Bombyx mandarina<\/em><\/a>, Manduca sexta<\/em><\/a>. <\/p>\n\n\n\n

There are 3 families of odorant binding proteins in mosquitoes and moths<\/strong>:<\/p>\n\n\n\n

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  1. the Classic<\/em> OBPs<\/li>\n\n\n\n
  2. the PlusC<\/em> OBPs<\/li>\n\n\n\n
  3. the Two-domains <\/em>also know as duplex<\/em> (OBPs formerly known as the Atypical <\/em>OBPs)<\/li>\n<\/ol>\n\n\n\n

    The hallmark of OBPs are their conserved 6 cysteines<\/strong> that forms 3 disulphide bridges<\/strong>.However the number of cysteines and the disulphide connectivity patterns of the OBPs vary among the different subfamilies. Click here for a graphical illustration<\/a>. A subgroup in the Classic<\/em> OBPs called the MinusC<\/em> OBPs and a subgroup in the two domain <\/em>OBP subfamily called the matype2<\/em> do not have all the six conserved cysteines in their OBP domains. Atypical<\/strong><\/em> odorant binding proteins are in fact two-domain or duplex OBPs<\/strong>, where each domain is distantly related to the Classic<\/em> OBPs.<\/p>\n\n\n\n

    We are providing in this database<\/p>\n\n\n\n