1E0E

N-terminal zinc-binding HHCC domain of HIV-2 integrase

「1AUB」から置き換えられました

1E0E の概要

• エントリーDOI: 10.2210/pdb1e0e/pdb
• NMR情報: BMRB: 4619
• 分子名称: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 INTEGRASE, ZINC ION (2 entities in total)
• 機能のキーワード: integrase, aids, polyprotein, dimer, zinc-binding protein, helix-turn-helix motif
• 由来する生物種: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (ISOLATE ROD) (HIV-2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12662.90

構造登録者

Eijkelenboom, A.P.A.M.,Van Den ent, F.M.I.,Plasterk, R.H.A.,Kaptein, R.,Boelens, R. (登録日: 2000-03-25, 公開日: 2001-03-19, 最終更新日: 2024-05-15)

主引用文献

Eijkelenboom, A.P.A.M.,Van Den Ent, F.M.I.,Wechselberger, R.,Plasterk, R.H.A.,Kaptein, R.,Boelens, R.
Refined Solution Structure of the Dimeric N-Terminal Hhcc Domain of HIV-2 Integrase
J.Biomol.NMR, 18:119-, 2000

PubMed Abstract: The solution structure of the dimeric N-terminal domain of HIV-2 integrase (residues 1-55, named IN(1-55)) has been determined using NMR spectroscopy. The structure of the monomer, which was already reported previously [Eijkelenboom et al. (1997) Curr. Biol., 7, 739-746], consists of four alpha-helices and is well defined. Helices alpha1, alpha2 and alpha3 form a three-helix bundle that is stabilized by zinc binding to His12, His16, Cys40 and Cys43. The dimer interface is formed by the N-terminal tail and the first half of helix alpha3. The orientation of the two monomeric units with respect to each other shows considerable variation. 15N relaxation studies have been used to characterize the nature of the intermonomeric disorder. Comparison of the dimer interface with that of the well-defined dimer interface of HIV-1 IN(1-55) shows that the latter is stabilized by additional hydrophobic interactions and a potential salt bridge. Similar interactions cannot be formed in HIV-2 IN(1-55) [Cai et al. (1997) Nat. Struct. Biol., 4, 567-577], where the corresponding residues are positively charged and neutral ones.

PubMed: 11101216
DOI: 10.1023/A:1008342312269

実験手法

SOLUTION NMR