1fb9: Difference between revisions
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==EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN== | ==EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN== | ||
<StructureSection load='1fb9' size='340' side='right' caption='[[1fb9]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1fb9' size='340' side='right' caption='[[1fb9]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fb9]] is a 1 chain structure | <table><tr><td colspan='2'>[[1fb9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FB9 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bku|1bku]], [[1byv|1byv]], [[1bzb|1bzb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bku|1bku]], [[1byv|1byv]], [[1bzb|1bzb]]</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=1fb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fb9 OCA], [http://pdbe.org/1fb9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fb9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fb9 PDBsum]</span></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=1fb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fb9 OCA], [http://pdbe.org/1fb9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fb9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fb9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fb9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1fb9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Dou, H]] | [[Category: Dou, H]] | ||
[[Category: Mao, J]] | [[Category: Mao, J]] | ||
Revision as of 13:56, 13 September 2017
EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONINEFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN
Structural highlights
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 PubMedSalmon calcitonin S-sulfonated analog (abbreviated as [S-SO(3)(-)]rsCT) was prepared by introducing two sulfonic groups into the side chains of Cys1 and Cys7 of recombinant salmon calcitonin. The hypocalcemic potency of this open-chain analog is 5500IU/mg, which is about 30% higher than that (4500IU/mg) of the wild type. The solution conformation of [S-SO(3)(-)]rsCT was studied in aqueous trifluoroethanol solution by CD, 2D-NMR spectroscopy, and distance geometry calculations. In the mixture of 60% TFE and 40% water, the peptide assumes an amphipathic alpha-helix in the region of residues 4-22, which is one turn longer than that of the native sCT. The structural feature analysis of the peptide revealed the presence of hydrophobic surface composed of five hydrophobic side chains of residues Leu4, Leu9, Leu12, Leu16, and Leu19, and a network of salt-bridges that consisted of a tetrad of oppositely charged side chains (Cys7-SO(3)(-)-Lys11(+)-Glu15(-)-Lys18(+)). The multiple salt bridges resulted in the stabilization of the longer amphipathic alpha-helix. Meanwhile, the higher hypocalcemic potency of the peptide could be attributed to the array of hydrophobic side chains of five leucine residues of the amphipathic alpha-helix. Solution structure and biological activity of recombinant salmon calcitonin S-sulfonated analog.,Wang Y, Dou H, Cao C, Zhang N, Ma J, Mao J, Wu H Biochem Biophys Res Commun. 2003 Jun 27;306(2):582-9. PMID:12804605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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