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1b2d
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1b2d.png|left|200px]] | ||
| - | < | + | ==PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.35 COORDINATES)== |
| - | + | <StructureSection load='1b2d' size='340' side='right'caption='[[1b2d]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1b2d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B2D FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1b2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b2d OCA], [https://pdbe.org/1b2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b2d RCSB], [https://www.ebi.ac.uk/pdbsum/1b2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b2d ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/INS_PIG INS_PIG] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. | ||
| + | == 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/b2/1b2d_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=1b2d ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single conformation at pH </= 5.80, two conformations between pH 6.00 and 6.98 and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the conformation of GluB13 switches from one rotamer to another rotamer. Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational change. By pH 9.00 many residues have undergone relatively large shifts and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the observed and calculated structure factors and map correlation coefficients indicate that the porcine insulin structure changes gradually as a function of pH. | ||
| - | + | Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding.,Diao J Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):670-6. Epub 2003, Mar 25. PMID:12657786<ref>PMID:12657786</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1b2d" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Insulin 3D Structures|Insulin 3D Structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
| - | + | ||
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Caspar | + | [[Category: Caspar DLD]] |
| - | [[Category: Diao | + | [[Category: Diao JS]] |
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Current revision
PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.35 COORDINATES)
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