1nbl: Difference between revisions

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-{{Seed}}
-[[Image:1nbl.png|left|200px]]
-<!--
+==NMR Structure of Hellethionin D==
-The line below this paragraph, containing "STRUCTURE_1nbl", creates the "Structure Box" on the page.
+<StructureSection load='1nbl' size='340' side='right'caption='[[1nbl]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1nbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helleborus_purpurascens Helleborus purpurascens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbl OCA], [https://pdbe.org/1nbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbl RCSB], [https://www.ebi.ac.uk/pdbsum/1nbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbl ProSAT]</span></td></tr>
-{{STRUCTURE_1nbl|  PDB=1nbl  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/THND_HELPU THND_HELPU] Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nbl_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1nbl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thionins are relatively small-sized multiple-cystine peptides that are probably involved in the plant defense against pathogens. As such, these peptides constitute promising candidates for engineered plant resistance in the agricultural industry. More recently, thionins have been proposed as potential immunotoxins in tumor therapy. In the search for pharmacologically active natural products, a new family of thionins was recently discovered in the roots of Helleborus purpurascens that accordingly were termed hellethionins. The structural characterization by NMR of one representative member of this family, i.e., of hellethionin D, clearly reveals that thionins from different sources share a highly conserved overall fold. In fact, the well-defined 3D structure of hellethionin D is very similar to those reported so far for viscotoxins, purothionins, or crambin, although distinct differences could be detected in the C-terminal portion, especially for loop 36-39. These differences may derive from the unusual distribution of charged residues in the C-terminal half of the peptide sequence compared to other thionins and from the uncommon occurrence of four contiguous threonine residues in loop 36-39. As expected, reduction of the disulfide bonds in hellethionin D leads to complete unfolding, but upon oxidative refolding by air oxygen in the presence of glutathione the correct isomer is recovered in high yields, confirming the very robust fold of this class of bioactive cystine peptides.
-===NMR Structure of Hellethionin D===
+Structural characterization of hellethionins from Helleborus purpurascens.,Milbradt AG, Kerek F, Moroder L, Renner C Biochemistry. 2003 Mar 4;42(8):2404-11. PMID:12600207<ref>PMID:12600207</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12600207}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1nbl" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12600207 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12600207}}
+__TOC__
+</StructureSection>
-==About this Structure==
-NBL is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Helleborus_purpurascens Helleborus purpurascens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBL OCA].
-==Reference==
-<ref group="xtra">PMID:12600207</ref><references group="xtra"/>
 [[Category: Helleborus purpurascens]]
-[[Category: Kerek, F.]]
+[[Category: Large Structures]]
-[[Category: Milbradt, A G.]]
+[[Category: Kerek F]]
-[[Category: Moroder, L.]]
+[[Category: Milbradt AG]]
-[[Category: Renner, C.]]
+[[Category: Moroder L]]
-[[Category: Gamma thionins helleborus]]
+[[Category: Renner C]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 22:43:02 2009''