3UQI
Crystallographic structure of FKBP12 from Aedes aegypti
Summary for 3UQI
| Entry DOI | 10.2210/pdb3uqi/pdb |
| Descriptor | FKBP-type peptidyl-prolyl cis-trans isomerase, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | fkbp12, isomerase, fk506 binding |
| Biological source | Aedes aegypti (Yellowfever mosquito) |
| Total number of polymer chains | 1 |
| Total formula weight | 11858.39 |
| Authors | Sreekanth, R.,Saw, K.Q.,Yoon, H.S. (deposition date: 2011-11-20, release date: 2012-06-27, Last modification date: 2023-11-01) |
| Primary citation | Rajan, S.,Saw, K.Q.,Nguyen, Q.T.,Baek, K.,Yoon, H.S. High-resolution crystal structure of FKBP12 from Aedes aegypti. Protein Sci., 21:1080-1084, 2012 Cited by PubMed 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. PubMed: 22517662DOI: 10.1002/pro.2079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.302 Å) |
Structure validation
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