1fb9: Difference between revisions

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New page: left|200px<br /><applet load="1fb9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fb9" /> '''EFFECTS OF S-SULFONATION ON THE SOLUTION STR...
 
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[[Image:1fb9.gif|left|200px]]<br /><applet load="1fb9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fb9" />
'''EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN'''<br />


==Overview==
==EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN==
Salmon 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.
<StructureSection load='1fb9' size='340' side='right'caption='[[1fb9]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1fb9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncorhynchus_gorbuscha Oncorhynchus gorbuscha]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1FB9 FirstGlance]. <br>
1FB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_gorbuscha Oncorhynchus gorbuscha]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FB9 OCA].  
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fb9 OCA], [https://pdbe.org/1fb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fb9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fb9 ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12804605 12804605]
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8QG84_ONCGO Q8QG84_ONCGO]
== 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/fb/1fb9_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=1fb9 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oncorhynchus gorbuscha]]
[[Category: Oncorhynchus gorbuscha]]
[[Category: Single protein]]
[[Category: Dou H]]
[[Category: Dou, H.]]
[[Category: Mao J]]
[[Category: Mao, J.]]
[[Category: Wang Y]]
[[Category: Wang, Y.]]
[[Category: Wu H]]
[[Category: Wu, H.]]
[[Category: alpha helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:35:22 2007''

Latest revision as of 13:12, 20 March 2024

EFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONINEFFECTS OF S-SULFONATION ON THE SOLUTION STRUCTURE OF SALMON CALCITONIN

Structural highlights

1fb9 is a 1 chain structure with sequence from Oncorhynchus gorbuscha. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8QG84_ONCGO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Drag the structure with the mouse to rotate

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OCA
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