1lpc
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene> | |LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'>CMP</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lp8|1LP8]], [[1lpd|1LPD]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpc OCA], [http://www.ebi.ac.uk/pdbsum/1lpc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lpc RCSB]</span> | ||
}} | }} | ||
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[[Category: Rajamohan, F.]] | [[Category: Rajamohan, F.]] | ||
[[Category: Uckun, F M.]] | [[Category: Uckun, F M.]] | ||
| - | [[Category: CMP]] | ||
[[Category: anti-hiv agent]] | [[Category: anti-hiv agent]] | ||
[[Category: dianthin antiviral protein]] | [[Category: dianthin antiviral protein]] | ||
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[[Category: ribosome inactivating protein]] | [[Category: ribosome inactivating protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:38 2008'' |
Revision as of 19:05, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Related: | 1LP8, 1LPD
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)
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
1LPC 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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