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==CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN== | |||
<StructureSection load='1wav' size='340' side='right'caption='[[1wav]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wav]] is a 12 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=1WAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAV 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPH:PHENOL'>IPH</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1wav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wav OCA], [https://pdbe.org/1wav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wav RCSB], [https://www.ebi.ac.uk/pdbsum/1wav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wav 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/wa/1wav_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=1wav ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The form-B monoclinic insulin crystal was obtained from the sodium citrate buffer with 1% zinc chloride, keeping phenolic content between 0.76% and 1.25%. Its space group is P2(1), cell constants are: a = 4.924 nm, b = 6.094 nm, c = 4.818 nm, beta = 95.8 degrees. There are 6 insulin molecules which form a hexamer. The initial phase was obtained by using rotation function program of X-PLOR program package and molecular packing program of our laboratory. The molecular model was chosen from 4 zinc bovine insulin hexamer. After the preliminary refinement by using the macromolecular rigid body refinement technique, the molecular model was further refined and adjusted by using the energy-minimizing stereochemically restrained least-squared refinement on the difference Fourier maps. The final R-factor is 22.4% at 0.3 nm resolution, the r.m.s. deviations from standard bond length and bond angle are 0.0022 nm and 4.7 degrees, respectively. | |||
Molecular replacement study on form-B monoclinic crystal of insulin.,Ding J, Wan Z, Chang W, Liang D Sci China C Life Sci. 1996 Apr;39(2):144-53. PMID:8760462<ref>PMID:8760462</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1wav" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Insulin 3D Structures|Insulin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Chang | [[Category: Chang W-R]] | ||
[[Category: Ding | [[Category: Ding J-H]] | ||
[[Category: Liang | [[Category: Liang D-C]] | ||
[[Category: Wan | [[Category: Wan Z-L]] | ||
Latest revision as of 10:34, 30 October 2024
CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULINCRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN
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 PubMedThe form-B monoclinic insulin crystal was obtained from the sodium citrate buffer with 1% zinc chloride, keeping phenolic content between 0.76% and 1.25%. Its space group is P2(1), cell constants are: a = 4.924 nm, b = 6.094 nm, c = 4.818 nm, beta = 95.8 degrees. There are 6 insulin molecules which form a hexamer. The initial phase was obtained by using rotation function program of X-PLOR program package and molecular packing program of our laboratory. The molecular model was chosen from 4 zinc bovine insulin hexamer. After the preliminary refinement by using the macromolecular rigid body refinement technique, the molecular model was further refined and adjusted by using the energy-minimizing stereochemically restrained least-squared refinement on the difference Fourier maps. The final R-factor is 22.4% at 0.3 nm resolution, the r.m.s. deviations from standard bond length and bond angle are 0.0022 nm and 4.7 degrees, respectively. Molecular replacement study on form-B monoclinic crystal of insulin.,Ding J, Wan Z, Chang W, Liang D Sci China C Life Sci. 1996 Apr;39(2):144-53. PMID:8760462[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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