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1lp8
From Proteopedia
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| , resolution 1.65Å | |||||||
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| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT
Overview
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.
About this Structure
1LP8 is a Single protein structure of sequence from Dianthus caryophyllus. Full crystallographic information is available from OCA.
Reference
High resolution X-ray structure and potent anti-HIV activity of recombinant dianthin antiviral protein., Kurinov IV, Rajamohan F, Uckun FM, Arzneimittelforschung. 2004;54(10):692-702. PMID:15553110
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