1ho0

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{{Seed}}
 
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[[Image:1ho0.png|left|200px]]
 
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==NEW B-CHAIN MUTANT OF BOVINE INSULIN==
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The line below this paragraph, containing "STRUCTURE_1ho0", creates the "Structure Box" on the page.
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<StructureSection load='1ho0' size='340' side='right'caption='[[1ho0]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ho0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HO0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ho0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho0 OCA], [https://pdbe.org/1ho0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho0 ProSAT]</span></td></tr>
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{{STRUCTURE_1ho0| PDB=1ho0 | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ho/1ho0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ho0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure of a new B-chain mutant of bovine insulin, in which the cysteines B7 and B19 are replaced by two serines, has been determined by circular dichroism, 2D-NMR and molecular modeling. This structure is compared with that of the oxidized B-chain of bovine insulin [Hawkins et al. (1995) Int. J. Peptide Protein Res.46, 424-433]. Circular dichroism spectroscopy showed in particular that a higher percentage of helical secondary structure for the B-chain mutant is estimated in trifluoroethanol solution in comparison with the oxidized B-chain. 2D-NMR experiments confirmed, among multiple conformations, that the B-chain mutant presents defined secondary structures such as a alpha-helix between residues B9 and B19, and a beta-turn between amino acids B20 and B23 in aqueous trifluoroethanol. The 3D structures, which are consistent with NMR data and were obtained using a simulated annealing protocol, showed that the tertiary structure of the B-chain mutant is better resolved and is more in agreement with the insulin crystal structure than the oxidized B-chain structure described by Hawkins et al. An explanation could be the presence of two sulfonate groups in the oxidized insulin B-chain. Either by their charges and/or their size, such chemical groups could play a destructuring effect and thus could favor peptide flexibility and conformational averaging. Thus, this study provides new insights on the folding of isolated B-chains.
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===NEW B-CHAIN MUTANT OF BOVINE INSULIN===
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A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure.,Dupradeau FY, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti JP J Pept Res. 2002 Jul;60(1):56-64. PMID:12081626<ref>PMID:12081626</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ho0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12081626}}, adds the Publication Abstract to the page
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*[[Insulin 3D Structures|Insulin 3D Structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12081626 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12081626}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Bos taurus]]
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1HO0 is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA].
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[[Category: Large Structures]]
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[[Category: Dupradeau FY]]
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==Reference==
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[[Category: Le Flem G]]
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<ref group="xtra">PMID:12081626</ref><references group="xtra"/>
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[[Category: Monti JP]]
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[[Category: Dupradeau, F Y.]]
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[[Category: Oulyadi H]]
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[[Category: Flem, G Le.]]
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[[Category: Prigent Y]]
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[[Category: Monti, J P.]]
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[[Category: Richard T]]
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[[Category: Oulyadi, H.]]
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[[Category: Prigent, Y.]]
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[[Category: Richard, T.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:07:18 2009''
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Current revision

NEW B-CHAIN MUTANT OF BOVINE INSULIN

PDB ID 1ho0

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