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| | ==Polycrystalline T6 Bovine Insulin: Anisotropic Lattice Evolution and Novel Structure Refinement Strategy== | | ==Polycrystalline T6 Bovine Insulin: Anisotropic Lattice Evolution and Novel Structure Refinement Strategy== |
| - | <StructureSection load='4idw' size='340' side='right'caption='[[4idw]]' scene=''> | + | <StructureSection load='4idw' size='340' side='right'caption='[[4idw]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4idw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IDW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4idw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IDW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idw OCA], [http://pdbe.org/4idw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4idw RCSB], [http://www.ebi.ac.uk/pdbsum/4idw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4idw ProSAT]</span></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=4idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idw OCA], [https://pdbe.org/4idw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4idw RCSB], [https://www.ebi.ac.uk/pdbsum/4idw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4idw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN]] 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. | + | [https://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Molecular Playground/Insulin|Molecular Playground/Insulin]] | + | *[[Insulin 3D Structures|Insulin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dreele, R B.Von]]
| + | [[Category: Fitch A]] |
| - | [[Category: Fitch, A]] | + | [[Category: Giannopoulou AE]] |
| - | [[Category: Giannopoulou, A E]] | + | [[Category: Knight L]] |
| - | [[Category: Knight, L]] | + | [[Category: Margiolaki I]] |
| - | [[Category: Margiolaki, I]] | + | [[Category: Norrman M]] |
| - | [[Category: Norrman, M]] | + | [[Category: Schluckebier G]] |
| - | [[Category: Schluckebier, G]] | + | [[Category: Von Dreele RB]] |
| - | [[Category: Wright, J P]] | + | [[Category: Wright JP]] |
| - | [[Category: Carbohydrate metabolism]] | + | |
| - | [[Category: Hormone]]
| + | |
| - | [[Category: Hormone-growth]]
| + | |
| - | [[Category: Insulin family]]
| + | |
| - | [[Category: T6 bovine insulin]]
| + | |
| Structural highlights
Function
INS_BOVIN 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.
Publication Abstract from PubMed
A series of bovine insulin samples were obtained as 14 polycrystalline precipitates at room temperature in the pH range 5.0-7.6. High-resolution powder X-ray diffraction data were collected to reveal the T6 hexameric insulin form. Sample homogeneity and reproducibility were verified by additional synchrotron measurements using an area detector. Pawley analyses of the powder patterns displayed pH- and radiation-induced anisotropic lattice modifications. The pronounced anisotropic lattice variations observed for T6 insulin were exploited in a 14-data-set Rietveld refinement to obtain an average crystal structure over the pH range investigated. Only the protein atoms of the known structure with PDB code 2a3g were employed in our starting model. A novel approach for refining protein structures using powder diffraction data is presented. In this approach, each amino acid is represented by a flexible rigid body (FRB). The FRB model requires a significantly smaller number of refinable parameters and restraints than a fully free-atom refinement. A total of 1542 stereochemical restraints were imposed in order to refine the positions of 800 protein atoms, two Zn atoms and 44 water molecules in the asymmetric unit using experimental data in the resolution range 18.2-2.7 A for all profiles.
High-resolution powder X-ray data reveal the T6 hexameric form of bovine insulin.,Margiolaki I, Giannopoulou AE, Wright JP, Knight L, Norrman M, Schluckebier G, Fitch AN, Von Dreele RB Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):978-90. doi:, 10.1107/S0907444913003867. Epub 2013 May 11. PMID:23695242[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Margiolaki I, Giannopoulou AE, Wright JP, Knight L, Norrman M, Schluckebier G, Fitch AN, Von Dreele RB. High-resolution powder X-ray data reveal the T6 hexameric form of bovine insulin. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):978-90. doi:, 10.1107/S0907444913003867. Epub 2013 May 11. PMID:23695242 doi:10.1107/S0907444913003867
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