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1LPC

HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)

Summary for 1LPC
Entry DOI10.2210/pdb1lpc/pdb
Related1LP8 1LPD
DescriptorDIANTHIN 30, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
Functional Keywordsdianthin antiviral protein, ribosome inactivating protein, anti-hiv agent, hiv-1 integrase inhibitor, polynucleotide:adenosine glycosidase, antiviral protein
Biological sourceDianthus caryophyllus (clove pink)
Total number of polymer chains1
Total formula weight28932.79
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 citationKurinov, 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: 15553110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

237735

数据于2025-06-18公开中

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