3KKS
Crystal structure of catalytic core domain of BIV integrase in crystal form II
Summary for 3KKS
| Entry DOI | 10.2210/pdb3kks/pdb |
| Related | 3KKR |
| Descriptor | Integrase, ACETATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta-strands flanked by alpha-helices, dna binding protein |
| Biological source | Bovine immunodeficiency virus (BIV) |
| Cellular location | Matrix protein p16: Virion (Potential). Capsid protein p26: Virion (Potential): P19560 |
| Total number of polymer chains | 2 |
| Total formula weight | 34450.94 |
| Authors | Shen, Y. (deposition date: 2009-11-06, release date: 2010-09-22, Last modification date: 2023-11-01) |
| Primary citation | Yao, X.,Fang, S.,Qiao, W.,Geng, Y.,Shen, Y. Crystal structures of catalytic core domain of BIV integrase: implications for the interaction between integrase and target DNA Protein Cell, 1:363-370, 2010 Cited by PubMed Abstract: Integrase plays a critical role in the recombination of viral DNA into the host genome. Therefore, over the past decade, it has been a hot target of drug design in the fight against type 1 human immunodeficiency virus (HIV-1). Bovine immunodeficiency virus (BIV) integrase has the same function as HIV-1 integrase. We have determined crystal structures of the BIV integrase catalytic core domain (CCD) in two different crystal forms at a resolution of 2.45 Å and 2.2 Å, respectively. In crystal form I, BIV integrase CCD forms a back-to-back dimer, in which the two active sites are on opposite sides. This has also been seen in many of the CCD structures of HIV-1 integrase that were determined previously. However, in crystal form II, BIV integrase CCD forms a novel face-to-face dimer in which the two active sites are close to each other. Strikingly, the distance separating the two active sites is approximately 20 Å, a distance that perfectly matches a 5-base pair interval. Based on these data, we propose a model for the interaction of integrase with its target DNA, which is also supported by many published biochemical data. Our results provide important clues for designing new inhibitors against HIV-1. PubMed: 21203948DOI: 10.1007/s13238-010-0047-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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