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New page: left|200px<br /><applet load="1b2f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b2f, resolution 1.90Å" /> '''PH AFFECTS GLU B13 S... |
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== | ==PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.98 COORDINATES)== | ||
Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH | <StructureSection load='1b2f' size='340' side='right'caption='[[1b2f]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1b2f]] 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=1B2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B2F 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]] 1.9Å</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=1b2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b2f OCA], [https://pdbe.org/1b2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b2f RCSB], [https://www.ebi.ac.uk/pdbsum/1b2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b2f 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/b2/1b2f_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1b2f 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> | |||
[[Category: | <div class="pdbe-citations 1b2f" 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]] | ||
Latest revision as of 02:18, 28 December 2023
PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.98 COORDINATES)PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.98 COORDINATES)
Structural highlights
FunctionINS_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStructures 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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