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[[Image:1ho0.jpg|left|200px]]
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{{STRUCTURE_1ho0|  PDB=1ho0  |  SCENE=  }}
'''NEW B-CHAIN MUTANT OF BOVINE INSULIN'''


==NEW B-CHAIN MUTANT OF BOVINE INSULIN==
<StructureSection load='1ho0' size='340' side='right'caption='[[1ho0]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
</table>
== Function ==
[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.
== 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/ho/1ho0_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=1ho0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HO0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA].
</div>
<div class="pdbe-citations 1ho0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12081626 12081626]
*[[Insulin 3D Structures|Insulin 3D Structures]]
[[Category: Single protein]]
== References ==
[[Category: Dupradeau, F Y.]]
<references/>
[[Category: Flem, G Le.]]
__TOC__
[[Category: Monti, J P.]]
</StructureSection>
[[Category: Oulyadi, H.]]
[[Category: Bos taurus]]
[[Category: Prigent, Y.]]
[[Category: Large Structures]]
[[Category: Richard, T.]]
[[Category: Dupradeau FY]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:03:20 2008''
[[Category: Le Flem G]]
[[Category: Monti JP]]
[[Category: Oulyadi H]]
[[Category: Prigent Y]]
[[Category: Richard T]]

Latest revision as of 08:32, 22 May 2024

NEW B-CHAIN MUTANT OF BOVINE INSULIN

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