8CT5
Catalytic Core Domain of HIV-1 Integrase (F185K)
Summary for 8CT5
| Entry DOI | 10.2210/pdb8ct5/pdb |
| Descriptor | Integrase, SULFATE ION (3 entities in total) |
| Functional Keywords | viral dna integration, dna binding, ledgf binding, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 18278.40 |
| Authors | Gupta, K.,Van Duyne, G.D.,Eilers, G. (deposition date: 2022-05-13, release date: 2023-02-15, Last modification date: 2024-10-30) |
| Primary citation | Eilers, G.,Gupta, K.,Allen, A.,Montermoso, S.,Murali, H.,Sharp, R.,Hwang, Y.,Bushman, F.D.,Van Duyne, G. Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 angstrom resolution: Routes to inhibitor optimization. Plos Pathog., 19:e1011097-e1011097, 2023 Cited by PubMed Abstract: HIV integrase (IN) inserts viral DNA into the host genome and is the target of the strand transfer inhibitors (STIs), a class of small molecules currently in clinical use. Another potent class of antivirals is the allosteric inhibitors of integrase, or ALLINIs. ALLINIs promote IN aggregation by stabilizing an interaction between the catalytic core domain (CCD) and carboxy-terminal domain (CTD) that undermines viral particle formation in late replication. Ongoing challenges with inhibitor potency, toxicity, and viral resistance motivate research to understand their mechanism. Here, we report a 2.93 Å X-ray crystal structure of the minimal ternary complex between CCD, CTD, and the ALLINI BI-224436. This structure reveals an asymmetric ternary complex with a prominent network of π-mediated interactions that suggest specific avenues for future ALLINI development and optimization. PubMed: 36867659DOI: 10.1371/journal.ppat.1011097 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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