2X2D
acetyl-CypA:HIV-1 N-term capsid domain complex
Summary for 2X2D
| Entry DOI | 10.2210/pdb2x2d/pdb |
| Related | 1AK4 1AWQ 1AWR 1AWS 1AWT 1AWU 1AWV 1BCK 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1FGL 1M63 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y 1MF8 1MIK 1NMK 1OCA 1RMH 1VBS 1VBT 1W8L 1W8M 1W8V 2ALF 2C55 2CPL 2CYH 2RMA 2RMB 2X25 2X2A 2X2C 3CYH 3CYS 4CYH 5CYH |
| Descriptor | PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, CAPSID PROTEIN P24 (3 entities in total) |
| Functional Keywords | isomerase-viral protein complex, isomerase viral protein complex, viral protein, isomerase, host-virus interaction, isomerase/viral protein |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Cytoplasm : P62937 Gag polyprotein: Host cell membrane; Lipid- anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion : P12493 |
| Total number of polymer chains | 4 |
| Total formula weight | 68826.60 |
| Authors | Lammers, M.,Neumann, H.,Chin, J.W.,James, L.C. (deposition date: 2010-01-12, release date: 2010-03-23, Last modification date: 2024-11-13) |
| Primary citation | Lammers, M.,Neumann, H.,Chin, J.W.,James, L.C. Acetylation Regulates Cyclophilin a Catalysis, Immunosuppression and HIV Isomerisation Nat.Chem.Biol., 6:331-, 2010 Cited by PubMed Abstract: Cyclophilin A (CypA) is a ubiquitous cis-trans prolyl isomerase with key roles in immunity and viral infection. CypA suppresses T-cell activation through cyclosporine complexation and is required for effective HIV-1 replication in host cells. We show that CypA is acetylated in diverse human cell lines and use a synthetically evolved acetyllysyl-tRNA synthetase/tRNA(CUA) pair to produce recombinant acetylated CypA in Escherichia coli. We determined atomic-resolution structures of acetylated CypA and its complexes with cyclosporine and HIV-1 capsid. Acetylation markedly inhibited CypA catalysis of cis to trans isomerization and stabilized cis rather than trans forms of the HIV-1 capsid. Furthermore, CypA acetylation antagonized the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. Our results reveal that acetylation regulates key functions of CypA in immunity and viral infection and provide a general set of mechanisms by which acetylation modulates interactions to regulate cell function. PubMed: 20364129DOI: 10.1038/NCHEMBIO.342 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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