1LP8

HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT

1LP8 の概要

• エントリーDOI: 10.2210/pdb1lp8/pdb
• 関連するPDBエントリー: 1LPC 1LPD
• 分子名称: DIANTHIN 30 (2 entities in total)
• 機能のキーワード: dianthin antiviral protein, ribosome inactivating protein, anti-hiv agent, hiv-1 integrase inhibitor, polynucleotide:adenosine glycosidase, antiviral protein
• 由来する生物種: Dianthus caryophyllus (clove pink)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28603.59

構造登録者

Kurinov, I.V.,Rajamohan, F.,Uckun, F.M. (登録日: 2002-05-07, 公開日: 2004-05-11, 最終更新日: 2024-04-03)

主引用文献

Kurinov, I.V.,Rajamohan, F.,Uckun, F.M.
High resolution X-ray structure and potent anti-HIV activity of recombinant dianthin antiviral protein.
Arzneimittelforschung, 54:692-702, 2004

PubMed Abstract: Dianthin antiviral protein (DAP) is a naturally occurring antiviral protein from the leaves of carnation (Dianthus caryophyllus) capable of depurinating HIV-1 RNA and inhibiting HIV-1 replication in human peripheral blood mononuclear cells. Escherichia coli-derived recombinant DAP (rDAP, amino acids 1-254) was purified to homogeneity for structural and functional studies. In the following paper the X-ray crystal structure of rDAP as well as its complexes with cyclic AMP and adenyl-guanosine (ApG) as substrate analogs at 1.7 A resolution are reported. Molecular modeling studies of the interactions of DAP and the structurally similar pokeweed antiviral protein (PAP) with a single-stranded RNA heptamer predicted a more potent anti-HIV activity for rDAP due to its unique surface topology and more favorable charge distribution in its 20 A-long RNA binding active center cleft. In accordance with the predictions of the modeling studies, rDAP was more potent than rPAP in depurinating HIV-1 RNA. To the knowledge of the authors, this is the first structural and functional characterization of recombinant DAP.

PubMed: 15553110

実験手法

X-RAY DIFFRACTION (1.65 Å)