1LPC
HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)
Summary for 1LPC
Entry DOI | 10.2210/pdb1lpc/pdb |
Related | 1LP8 1LPD |
Descriptor | DIANTHIN 30, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total) |
Functional Keywords | dianthin antiviral protein, ribosome inactivating protein, anti-hiv agent, hiv-1 integrase inhibitor, polynucleotide:adenosine glycosidase, antiviral protein |
Biological source | Dianthus caryophyllus (clove pink) |
Total number of polymer chains | 1 |
Total formula weight | 28932.79 |
Authors | Kurinov, I.V.,Rajamohan, F.,Uckun, F.M. (deposition date: 2002-05-07, release date: 2004-05-11, Last modification date: 2023-08-16) |
Primary citation | 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 Cited by 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: 15553110PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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