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1lp8
From Proteopedia
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[[Image:1lp8.gif|left|200px]] | [[Image:1lp8.gif|left|200px]] | ||
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'''HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT''' | '''HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT''' | ||
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[[Category: Dianthus caryophyllus]] | [[Category: Dianthus caryophyllus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: | + | [[Category: RRNA N-glycosylase]] |
[[Category: Kurinov, I V.]] | [[Category: Kurinov, I V.]] | ||
[[Category: Rajamohan, F.]] | [[Category: Rajamohan, F.]] | ||
[[Category: Uckun, F M.]] | [[Category: Uckun, F M.]] | ||
| - | [[Category: | + | [[Category: Anti-hiv agent]] |
| - | [[Category: | + | [[Category: Dianthin antiviral protein]] |
| - | [[Category: | + | [[Category: Hiv-1 integrase inhibitor]] |
| - | [[Category: | + | [[Category: Polynucleotide:adenosine glycosidase]] |
| - | [[Category: | + | [[Category: Ribosome inactivating protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:08:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:08, 2 May 2008
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 Page seeded by OCA on Sat May 3 00:08:30 2008
