Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/97150
Title: | High-resolution crystal structure of FKBP12 from Aedes aegypti | Authors: | Rajan, Sreekanth Saw, Kai Qian Nguyen, Quoc Toan Baek, Kwanghee Yoon, Ho Sup |
Keywords: | DRNTU::Science::Biological sciences | Issue Date: | 2012 | Source: | Rajan, 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. | Series/Report no.: | Protein science | 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. | URI: | https://hdl.handle.net/10356/97150 http://hdl.handle.net/10220/10490 |
ISSN: | 0961-8368 | DOI: | 10.1002/pro.2079 | Rights: | © 2012 The Protein Society. | Fulltext Permission: | none | Fulltext Availability: | No Fulltext |
Appears in Collections: | SBS Journal Articles |
SCOPUSTM
Citations
50
5
Updated on Mar 28, 2023
Web of ScienceTM
Citations
50
5
Updated on Mar 24, 2023
Page view(s) 10
730
Updated on Mar 29, 2023
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.