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3ins
From Proteopedia
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| - | {{STRUCTURE_3ins| PDB=3ins | SCENE= }} | ||
| - | ===STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT=== | ||
| - | {{ABSTRACT_PUBMED_2695122}} | ||
| - | == | + | ==STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT== |
| - | [[http://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. | + | <StructureSection load='3ins' size='340' side='right'caption='[[3ins]], [[Resolution|resolution]] 1.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ins]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3INS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3INS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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=3ins FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ins OCA], [https://pdbe.org/3ins PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ins RCSB], [https://www.ebi.ac.uk/pdbsum/3ins PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ins 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/in/3ins_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=3ins ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Neutron diffraction data for porcine 2Zn insulin were collected to 2.2 A resolution from a single crystal deuterated by slow exchange of mother liquor. A joint neutron/X-ray restrained-least-squares refinement was undertaken using the neutron data, as well as the 1.5 A resolution X-ray data collected previously. The final R factors were 0.182 for the X-ray data and 0.191 for the neutron data. Resulting atomic coordinates were compared with the initial X-ray model, showing a total r.m.s. shift of 0.36 A for the protein and 0.6 A for the solvent. Protonation of a number of individual amino acids was investigated by analysis of the neutron maps. No D atoms were found between the carboxylates of Glu B13 which make an intermolecular contact, suggesting nonbonded interaction rather than the predicted hydrogen bond. Amide hydrogen exchange was investigated in a refinement of their atomic occupancies. Regions of unexchanged amide groups were found in the center of the B helices. The results of this study emphasize the limited amount of information available in neutron diffraction studies of proteins at resolution lower than 2 A. | ||
| - | + | Structure of insulin: results of joint neutron and X-ray refinement.,Wlodawer A, Savage H, Dodson G Acta Crystallogr B. 1989 Feb 1;45 ( Pt 1):99-107. PMID:2695122<ref>PMID:2695122</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 3ins" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Insulin 3D Structures|Insulin 3D Structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pig]] | [[Category: Pig]] | ||
| - | [[Category: Savage, H | + | [[Category: Savage, H]] |
| - | [[Category: Wlodawer, A | + | [[Category: Wlodawer, A]] |
[[Category: Hormone]] | [[Category: Hormone]] | ||
Current revision
STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT
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Categories: Large Structures | Pig | Savage, H | Wlodawer, A | Hormone
