1K6Y
Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase
1K6Y の概要
| エントリーDOI | 10.2210/pdb1k6y/pdb |
| 分子名称 | Integrase, ZINC ION, POTASSIUM ION, ... (5 entities in total) |
| 機能のキーワード | hiv-1, integrase, domain organization, transferase |
| 由来する生物種 | Human immunodeficiency virus 1 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 94075.87 |
| 構造登録者 | |
| 主引用文献 | Wang, J.Y.,Ling, H.,Yang, W.,Craigie, R. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. EMBO J., 20:7333-7343, 2001 Cited by PubMed Abstract: Retroviral integrase, an essential enzyme for replication of human immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains three structurally distinct domains, an N-terminal domain, the catalytic core and a C-terminal domain. To elucidate their spatial arrangement, we have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic core domains. This structure reveals a dimer interface between the N-terminal domains different from that observed for the isolated domain. It also complements the previously determined structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalytic core of the two structures results in a plausible full-length integrase dimer. Furthermore, an integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding. PubMed: 11743009DOI: 10.1093/emboj/20.24.7333 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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