6VRG
Structure of HIV-1 integrase with native amino-terminal sequence
Summary for 6VRG
| Entry DOI | 10.2210/pdb6vrg/pdb |
| Descriptor | Integrase, ZINC ION, POTASSIUM ION, ... (5 entities in total) |
| Functional Keywords | integrase, zinc ion binding, nucleic acid binding, dna integration, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 4 |
| Total formula weight | 94075.87 |
| Authors | Eilers, G.,Gupta, K.,Allen, A.,Zhou, J.,Hwang, Y.,Cory, M.,Bushman, F.D.,Van Duyne, G.D. (deposition date: 2020-02-07, release date: 2020-09-09, Last modification date: 2023-10-11) |
| Primary citation | Eilers, G.,Gupta, K.,Allen, A.,Zhou, J.,Hwang, Y.,Cory, M.B.,Bushman, F.D.,Van Duyne, G. Influence of the amino-terminal sequence on the structure and function of HIV integrase. Retrovirology, 17:28-28, 2020 Cited by PubMed Abstract: Antiretroviral therapy (ART) can mitigate the morbidity and mortality caused by the human immunodeficiency virus (HIV). Successful development of ART can be accelerated by accurate structural and biochemical data on targets and their responses to inhibitors. One important ART target, HIV integrase (IN), has historically been studied in vitro in a modified form adapted to bacterial overexpression, with a methionine or a longer fusion protein sequence at the N-terminus. In contrast, IN present in viral particles is produced by proteolytic cleavage of the Pol polyprotein, which leaves a phenylalanine at the N-terminus (IN 1F). Inspection of available structures suggested that added residues on the N-terminus might disrupt proper protein folding and formation of multimeric complexes. PubMed: 32867805DOI: 10.1186/s12977-020-00537-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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