Literature DB >> 22517662

High-resolution crystal structure of FKBP12 from Aedes aegypti.

Sreekanth Rajan1, Kai Qian Saw, Quoc Toan Nguyen, Kwanghee Baek, Ho Sup Yoon.   

Abstract

Dengue 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.
Copyright © 2012 The Protein Society.

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Year:  2012        PMID: 22517662      PMCID: PMC3403445          DOI: 10.1002/pro.2079

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  29 in total

1.  Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex.

Authors:  R A Aldape; O Futer; M T DeCenzo; B P Jarrett; M A Murcko; D J Livingston
Journal:  J Biol Chem       Date:  1992-08-15       Impact factor: 5.157

Review 2.  Dengue vaccine design: issues and challenges.

Authors:  M J Cardosa
Journal:  Br Med Bull       Date:  1998       Impact factor: 4.291

3.  The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors.

Authors:  T Wang; B Y Li; P D Danielson; P C Shah; S Rockwell; R J Lechleider; J Martin; T Manganaro; P K Donahoe
Journal:  Cell       Date:  1996-08-09       Impact factor: 41.582

4.  NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.

Authors:  Reema Alag; Insaf A Qureshi; Nagakumar Bharatham; Joon Shin; Julien Lescar; Ho Sup Yoon
Journal:  Protein Sci       Date:  2010-08       Impact factor: 6.725

5.  A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities.

Authors:  Paul Monaghan; Angus Bell
Journal:  Mol Biochem Parasitol       Date:  2005-02       Impact factor: 1.759

Review 6.  Role of FK506 binding proteins in neurodegenerative disorders.

Authors:  S Chattopadhaya; A Harikishore; H S Yoon
Journal:  Curr Med Chem       Date:  2011       Impact factor: 4.530

7.  Targeting FK506 binding proteins to fight malarial and bacterial infections: current advances and future perspectives.

Authors:  N Bharatham; M W Chang; H S Yoon
Journal:  Curr Med Chem       Date:  2011       Impact factor: 4.530

8.  FKBP38 protects Bcl-2 from caspase-dependent degradation.

Authors:  Bo-Hwa Choi; Lin Feng; Ho Sup Yoon
Journal:  J Biol Chem       Date:  2010-02-05       Impact factor: 5.157

9.  Mycophenolic acid inhibits dengue virus infection by preventing replication of viral RNA.

Authors:  Michael S Diamond; Marcus Zachariah; Eva Harris
Journal:  Virology       Date:  2002-12-20       Impact factor: 3.616

10.  Phaser crystallographic software.

Authors:  Airlie J McCoy; Ralf W Grosse-Kunstleve; Paul D Adams; Martyn D Winn; Laurent C Storoni; Randy J Read
Journal:  J Appl Crystallogr       Date:  2007-07-13       Impact factor: 3.304

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