1LP8

High resolution X-ray structure and potent anti-HIV activity of recombinant dianthin antiviral protein.

(2004) Arzneimittelforschung 54: 692-702

• PubMed: 15553110 Search on PubMed
• DOI: https://doi.org/10.1055/s-0031-1297024
• Primary Citation of Related Structures:  
  1LP8, 1LPC, 1LPD


• 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.

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Organizational Affiliation: 

Biotherapy and Drug Discovery Program, Parker Hughes Institute, St Paul, Minnesota 55113, USA.