3KKS

Crystal structure of catalytic core domain of BIV integrase in crystal form II

3KKS の概要

• エントリーDOI: 10.2210/pdb3kks/pdb
• 関連するPDBエントリー: 3KKR
• 分子名称: Integrase, ACETATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: beta-strands flanked by alpha-helices, dna binding protein
• 由来する生物種: Bovine immunodeficiency virus (BIV)
• 細胞内の位置: Matrix protein p16: Virion (Potential). Capsid protein p26: Virion (Potential): P19560
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34450.94

構造登録者

Shen, Y. (登録日: 2009-11-06, 公開日: 2010-09-22, 最終更新日: 2023-11-01)

主引用文献

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

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: 21203948
DOI: 10.1007/s13238-010-0047-5

実験手法

X-RAY DIFFRACTION (2.2 Å)