1brv: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1brv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_respiratory_syncytial_virus_(strain_391-2) Bovine respiratory syncytial virus (strain 391-2)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRV FirstGlance]. <br>
-</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 48 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=1brv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brv OCA], [https://pdbe.org/1brv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brv RCSB], [https://www.ebi.ac.uk/pdbsum/1brv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brv ProSAT]</span></td></tr>
 </table>
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brv_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <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=1brv ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues, lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses in both cattle and man.
+Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus.,Doreleijers JF, Langedijk JP, Hard K, Boelens R, Rullmann JA, Schaaper WM, van Oirschot JT, Kaptein R Biochemistry. 1996 Nov 26;35(47):14684-8. PMID:8942628<ref>PMID:8942628</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1brv" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>