This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lp8
From Proteopedia
OCA (Talk | contribs)
(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...)
Next diff →
Revision as of 12:11, 8 November 2007
|
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
Page seeded by OCA on Thu Nov 8 14:17:30 2007
