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1lpc

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(New page: 200px<br /> <applet load="1lpc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lpc, resolution 1.70&Aring;" /> '''HIGH RESOLUTION STR...)
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[[Image:1lpc.gif|left|200px]]<br />
 
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<applet load="1lpc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lpc, resolution 1.70&Aring;" />
 
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'''HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)'''<br />
 
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==Overview==
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==HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)==
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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.
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<StructureSection load='1lpc' size='340' side='right'caption='[[1lpc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lpc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dianthus_caryophyllus Dianthus caryophyllus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpc OCA], [https://pdbe.org/1lpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpc RCSB], [https://www.ebi.ac.uk/pdbsum/1lpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RIP0_DIACA RIP0_DIACA] Single-chain ribosome-inactivating protein.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lpc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15553110</ref>
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1LPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dianthus_caryophyllus Dianthus caryophyllus] with CMP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LPC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15553110 15553110]
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</div>
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[[Category: Dianthus caryophyllus]]
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<div class="pdbe-citations 1lpc" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: rRNA N-glycosylase]]
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[[Category: Kurinov, I.V.]]
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[[Category: Rajamohan, F.]]
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[[Category: Uckun, F.M.]]
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[[Category: CMP]]
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[[Category: anti-hiv agent]]
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[[Category: dianthin antiviral protein]]
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[[Category: hiv-1 integrase inhibitor]]
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[[Category: polynucleotide:adenosine glycosidase]]
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[[Category: ribosome inactivating protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:17:35 2007''
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==See Also==
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*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Dianthus caryophyllus]]
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[[Category: Large Structures]]
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[[Category: Kurinov IV]]
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[[Category: Rajamohan F]]
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[[Category: Uckun FM]]

Current revision

HIGH RESOLUTION STRUCTURE OF RECOMBINANT DIANTHIN ANTIVIRAL PROTEIN-POTENT ANTI-HIV AGENT (COMPLEX WITH CYCLIC AMP)

PDB ID 1lpc

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