1byv: Difference between revisions

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 ==GLYCOSYLATED EEL CALCITONIN==
-<StructureSection load='1byv' size='340' side='right'caption='[[1byv]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1byv' size='340' side='right'caption='[[1byv]]' scene=''>
 == Structural highlights ==
 <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>
-</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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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>
 <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.
+[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]]
@@ Line 20: / Line 20: @@
 </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.
-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>
-<div class="pdbe-citations 1byv" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Anguilla japonica]]
 [[Category: Large Structures]]
-[[Category: Haneda, K]]
+[[Category: Haneda K]]
-[[Category: Hashimoto, Y]]
+[[Category: Hashimoto Y]]
-[[Category: Inazu, T]]
+[[Category: Inazu T]]
-[[Category: Nishikido, J]]
+[[Category: Nishikido J]]
-[[Category: Opella, S J]]
+[[Category: Opella SJ]]
-[[Category: Toma, K]]
+[[Category: Toma K]]
-[[Category: Valentine, K G]]
+[[Category: Valentine KG]]
-[[Category: Yamamoto, K]]
+[[Category: Yamamoto K]]
-[[Category: Calcium-regulator]]
-[[Category: Hormone-growth factor complex]]
-[[Category: Horomone]]
-[[Category: Osteoporosis]]