dc.contributor.authorRajan, Sreekanth
dc.contributor.authorSaw, Kai Qian
dc.contributor.authorNguyen, Quoc Toan
dc.contributor.authorBaek, Kwanghee
dc.contributor.authorYoon, Ho Sup
dc.date.accessioned2013-06-19T07:17:30Z
dc.date.available2013-06-19T07:17:30Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationRajan, S., Saw, K. Q., Nguyen, Q. T., Baek, K., & Yoon, H. S. (2012). High-resolution crystal structure of FKBP12 from Aedes aegypti. Protein Science, 21(7), 1080-1084.en_US
dc.identifier.issn0961-8368en_US
dc.identifier.urihttp://hdl.handle.net/10220/10490
dc.description.abstractDengue is one of the most infectious viral diseases prevalent mainly in tropical countries. The virus is transmitted by Aedes species of mosquito, primarily Aedes aegypti. Dengue remains a challenging drug target for years as the virus eludes the immune responses. Currently, no vaccines or antiviral drugs are available for dengue prevention. Previous studies suggested that the immunosuppressive drug FK506 shows antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in the Plasmodium parasite. Likewise, a FKBP family protein has been identified in A. aegypti (AaFKBP12) in which AaFKBP12 is assumed to play a similar role in its life cycle. FKBPs belong to a highly conserved class of proteins and are considered as an attractive pharmacological target. Herein, we present a high-resolution crystal structure of AaFKBP12 at 1.3 Å resolution and discuss its structural features throwing light in facilitating the design of potential antagonists against the dengue-transmitting mosquito.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesProtein scienceen_US
dc.rights© 2012 The Protein Society.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleHigh-resolution crystal structure of FKBP12 from Aedes aegyptien_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1002/pro.2079


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