1lp8
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(New page: 200px<br /> <applet load="1lp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lp8, resolution 1.65Å" /> '''HIGH RESOLUTION STR...)
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Revision as of 12:11, 8 November 2007
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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. Active as rRNA N-glycosylase, with EC number 3.2.2.22 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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