1kvz

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{{Seed}}
 
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[[Image:1kvz.png|left|200px]]
 
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==Solution Structure of Cytotoxic RC-RNase4==
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The line below this paragraph, containing "STRUCTURE_1kvz", creates the "Structure Box" on the page.
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<StructureSection load='1kvz' size='340' side='right'caption='[[1kvz]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kvz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KVZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=1kvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kvz OCA], [https://pdbe.org/1kvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kvz RCSB], [https://www.ebi.ac.uk/pdbsum/1kvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kvz ProSAT]</span></td></tr>
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{{STRUCTURE_1kvz| PDB=1kvz | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9DFY6_AQUCT Q9DFY6_AQUCT]
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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/kv/1kvz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kvz 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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Cytotoxic ribonucleases with antitumor activity are mainly found in the oocytes and early embryos of frogs. Native RC-RNase 4 (RNase 4), consisting of 106 residues linked with four disulfide bridges, is a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana. RNase 4 belongs to the bovine pancreatic ribonuclease (RNase A) superfamily. Recombinant RC-RNase 4 (rRNase 4), which contains an additional Met residue and glutamine instead of pyroglutamate at the N terminus, was found to possess less catalytic and cytotoxic activities than RNase 4. Equilibrium thermal and guanidine-HCl denaturation CD measurements revealed that RNase 4 is more thermally and chemically stable than rRNase 4. However, CD and NMR data showed that there is no gross conformational change between native and recombinant RNase 4. The NMR solution structure of rRNase 4 was determined to comprise three alpha-helices and two sets of antiparallel beta-sheets. Superimposition of each structure with the mean structure yielded an average root mean square deviation (RMSD) of 0.72(+/-0.14)A for the backbone atoms, and 1.42(+/-0.19)A for the heavy atoms in residues 3-105. A comparison of the 3D structure of rRNase 4 with the structurally and functionally related cytotoxic ribonuclease, onconase (ONC), showed that the two H-bonds in the N-terminal pyroglutamate of ONC were not present at the corresponding glutamine residue of rRNase 4. We suggest that the loss of these two H-bonds is one of the key factors responsible for the reductions of the conformational stability, catalytic and cytotoxic activities in rRNase 4. Furthermore, the differences of side-chain conformations of subsite residues among RNase A, ONC and rRNase 4 are related to their distinct catalytic activities and base preferences.
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===Solution Structure of Cytotoxic RC-RNase4===
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Solution structure of the cytotoxic RNase 4 from oocytes of bullfrog Rana catesbeiana.,Hsu CH, Liao YD, Pan YR, Chen LW, Wu SH, Leu YJ, Chen C J Mol Biol. 2003 Feb 28;326(4):1189-201. PMID:12589762<ref>PMID:12589762</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kvz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12589762}}, adds the Publication Abstract to the page
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12589762 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12589762}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1KVZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVZ OCA].
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[[Category: Lithobates catesbeianus]]
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[[Category: Chen C]]
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==Reference==
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[[Category: Chen L-W]]
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Solution structure of the cytotoxic RNase 4 from oocytes of bullfrog Rana catesbeiana., Hsu CH, Liao YD, Pan YR, Chen LW, Wu SH, Leu YJ, Chen C, J Mol Biol. 2003 Feb 28;326(4):1189-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12589762 12589762]
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[[Category: Hsu C-H]]
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[[Category: Rana catesbeiana]]
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[[Category: Liao Y-D]]
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[[Category: Single protein]]
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[[Category: Wu S-H]]
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[[Category: Chen, C.]]
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[[Category: Chen, L W.]]
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[[Category: Hsu, C H.]]
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[[Category: Liao, Y D.]]
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[[Category: Wu, S H.]]
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[[Category: Antitumor]]
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[[Category: Bullfrog]]
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[[Category: Cytotoxicity,ribonuclease]]
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[[Category: Nmr]]
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[[Category: Structure from molmol]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:07:38 2008''
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Current revision

Solution Structure of Cytotoxic RC-RNase4

PDB ID 1kvz

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