1byv: Difference between revisions

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-{{Seed}}
-[[Image:1byv.png|left|200px]]
-<!--
+==GLYCOSYLATED EEL CALCITONIN==
-The line below this paragraph, containing "STRUCTURE_1byv", creates the "Structure Box" on the page.
+<StructureSection load='1byv' size='340' side='right'caption='[[1byv]]' 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'>[[1byv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BYV 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, 10 models</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-{{STRUCTURE_1byv|  PDB=1byv  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1byv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byv OCA], [https://pdbe.org/1byv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1byv RCSB], [https://www.ebi.ac.uk/pdbsum/1byv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1byv ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CALC_ANGJA CALC_ANGJA] Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.
+== 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/by/1byv_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=1byv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structures of eel calcitonin (CT) and two glycosylated CT derivatives, [Asn(GlcNAc)3]-CT (CT-GlcNAc) and [Asn(Man6-GlcNAc2)3]-CT (CT-M6), in micelles were determined by solution NMR spectroscopy. The topologies of these peptides associated with oriented lipid bilayers were determined with solid-state NMR. All of the peptides were found to have an identical conformation in micelles characterized by an amphipathic alpha-helix consisting of residues Ser5 through Leu19 followed by an unstructured region at the C-terminus. The overall conformation of the peptide moiety was not affected by the glycosylation. Nevertheless, comparison of the relative exchange rates of the Leu12 amide proton might suggest the possibility that fluctuations of the alpha-helix are reduced by glycosylation. The presence of NOEs between the carbohydrate and the peptide moieties of CT-GlcNAc and CT-M6 and the amide proton chemical shift data suggested that the carbohydrate interacted with the peptide, and this might account for the conformational stabilization of the alpha-helix. Both the unmodified CT and the glycosylated CT were found to have orientations with their helix axes parallel to the plane of the lipid bilayers by solid-state NMR spectroscopy.
-===GLYCOSYLATED EEL CALCITONIN===
+Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy.,Hashimoto Y, Toma K, Nishikido J, Yamamoto K, Haneda K, Inazu T, Valentine KG, Opella SJ Biochemistry. 1999 Jun 29;38(26):8377-84. PMID:10387083<ref>PMID:10387083</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_10387083}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1byv" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 10387083 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10387083}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BYV is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA].
-==Reference==
-<ref group="xtra">PMID:10387083</ref><references group="xtra"/>
 [[Category: Anguilla japonica]]
-[[Category: Haneda, K.]]
+[[Category: Large Structures]]
-[[Category: Hashimoto, Y.]]
+[[Category: Haneda K]]
-[[Category: Inazu, T.]]
+[[Category: Hashimoto Y]]
-[[Category: Nishikido, J.]]
+[[Category: Inazu T]]
-[[Category: Opella, S J.]]
+[[Category: Nishikido J]]
-[[Category: Toma, K.]]
+[[Category: Opella SJ]]
-[[Category: Valentine, K G.]]
+[[Category: Toma K]]
-[[Category: Yamamoto, K.]]
+[[Category: Valentine KG]]
-[[Category: Calcium-regulator]]
+[[Category: Yamamoto K]]
-[[Category: Horomone]]
-[[Category: Osteoporosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:44:37 2009''