2LPV
Solution Structure of FKBP12 from Aedes aegypti
Summary for 2LPV
| Entry DOI | 10.2210/pdb2lpv/pdb |
| NMR Information | BMRB: 18278 |
| Descriptor | FKBP-type peptidyl-prolyl cis-trans isomerase (1 entity in total) |
| Functional Keywords | fkbp12, isomerase |
| Biological source | Aedes aegypti (Yellowfever mosquito) |
| Total number of polymer chains | 1 |
| Total formula weight | 11553.06 |
| Authors | Chakraborty, G.,Shin, J. (deposition date: 2012-02-20, release date: 2013-02-06, Last modification date: 2024-05-15) |
| Primary citation | Chakraborty, G.,Shin, J.,Nguyen, Q.T.,Harikishore, A.,Baek, K.,Yoon, H.S. Solution structure of FK506-binding protein 12 from Aedes aegypti. Proteins, 80:2476-2481, 2012 Cited by PubMed 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. PubMed: 22806993DOI: 10.1002/prot.24146 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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