5H23
Crystal structure of Chikungunya virus capsid protein
Summary for 5H23
| Entry DOI | 10.2210/pdb5h23/pdb |
| Descriptor | Capsid Protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | chikungunya virus, capsid protein, viral protein |
| Biological source | Chikungunya virus (CHIKV) |
| Total number of polymer chains | 2 |
| Total formula weight | 35192.12 |
| Authors | Sharma, R.,Kesari, P.,Tomar, S.,Kumar, P. (deposition date: 2016-10-14, release date: 2018-03-14, Last modification date: 2023-11-08) |
| Primary citation | Sharma, R.,Kesari, P.,Kumar, P.,Tomar, S. Structure-function insights into chikungunya virus capsid protein: Small molecules targeting capsid hydrophobic pocket. Virology, 515:223-234, 2018 Cited by PubMed Abstract: The crystal structure of chikungunya (CHIKV) virus capsid protease domain has been determined at 2.2Å. Structure reveals a chymotrypsin-like protease fold with a conserved hydrophobic pocket in CHIKV capsid protein (CP) for interaction with the cytoplasmic tail of E2 (cdE2) similar to the capsid protein of other alphaviruses. Molecular contacts between CP-cdE2 were determined by fitting structures of CHIKV CP and cdE2 into the cryo-EM map of Venezuelan equine encephalitis virus (VEEV). Binding of (S)-(+)-Mandelic acid (MDA) and Ethyl 3-aminobenzoate (EAB) to the hydrophobic pocket of CP was evaluated by molecular docking. Surface plasmon resonance (SPR) and fluorescence spectroscopy experiments confirmed MDA and EAB binding to the CP. The binding constants (K) obtained from SPR for MDA and EAB were 1.2 × 10 M and 0.2 × 10 M, respectively. This study adds to the understanding of chikungunya virus structural proteins and may serve as the basis for antiviral development against chikungunya disease. PubMed: 29306785DOI: 10.1016/j.virol.2017.12.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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