Literature DB >> 22806993

Solution structure of FK506-binding protein 12 from Aedes aegypti.

Goutam Chakraborty1, Joon Shin, Quoc Toan Nguyen, Amaravadhi Harikishore, Kwanghee Baek, Ho Sup Yoon.   

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.
Copyright © 2012 Wiley Periodicals, Inc.

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Year:  2012        PMID: 22806993     DOI: 10.1002/prot.24146

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  1 in total

1.  Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia.

Authors:  Garry W Buchko; Stephen N Hewitt; Wesley C Van Voorhis; Peter J Myler
Journal:  J Biomol NMR       Date:  2013-11-29       Impact factor: 2.835

  1 in total

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