Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/98219
Title: Solution structure of FK506-binding protein 12 from Aedes aegypti
Authors: Chakraborty, Goutam
Shin, Joon
Nguyen, Quoc Toan
Harikishore, Amaravadhi
Baek, Kwanghee
Yoon, Ho Sup
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Chakraborty, G., Shin, J., Nguyen, Q. T., Harikishore, A., Baek, K., & Yoon, H. S. (2012). Solution structure of FK506-binding protein 12 from Aedes aegypti . Proteins: Structure, Function, and Bioinformatics, 80(10), 2476-2481.
Series/Report no.: Proteins: structure, function, and bioinformatics
Abstract: Dengue remains one of the major public concerns as the virus eludes the immune response. Currently, no vaccines or antiviral therapeutics are available for dengue prevention or treatment. Immunosuppressive drug FK506 shows an antimalarial activity, and its molecular target, FK506-binding protein (FKBP), was identified in human Plasmodium parasites. Likewise, a conserved FKBP family protein has also been identified in Aedes aegypti (AaFKBP12), which is expected to play a similar role in the life cycle of Aedes aegypti, the primary vector of dengue virus infection. As FKBPs belong to a highly conserved class of immunophilin family and are involved in key biological regulations, they are considered as attractive pharmacological targets. In this study, we have determined the nuclear magnetic resonance solution structure of AaFKBP12, a novel FKBP member from Aedes aegypti, and presented its structural features, which may facilitate the design of potential inhibitory ligands against the dengue-transmitting mosquitoes.
URI: https://hdl.handle.net/10356/98219
http://hdl.handle.net/10220/12368
ISSN: 0887-3585
DOI: http://dx.doi.org/10.1002/prot.24146
Rights: © 2012 Wiley Periodicals, Inc.
metadata.item.grantfulltext: none
metadata.item.fulltext: No Fulltext
Appears in Collections:SBS Journal Articles

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