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| | <StructureSection load='5i5c' size='340' side='right'caption='[[5i5c]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='5i5c' size='340' side='right'caption='[[5i5c]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i5c]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I5C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I5C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i5c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I5C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i5a|5i5a]], [[5i5b|5i5b]]</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=5i5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i5c OCA], [https://pdbe.org/5i5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i5c RCSB], [https://www.ebi.ac.uk/pdbsum/5i5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i5c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i5c OCA], [http://pdbe.org/5i5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i5c RCSB], [http://www.ebi.ac.uk/pdbsum/5i5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i5c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/K1A_STIHL K1A_STIHL]] Inhibits voltage-dependent potassium channels. Inhibits Kv1.3/KCNA3 potently and also blocks Kv1.1/KCNA1, Kv1.4/KCNA4, and Kv1.6/KCNA6 at subnanomolar concentrations.<ref>PMID:7660365</ref> | + | [https://www.uniprot.org/uniprot/K1A_STIHL K1A_STIHL] Inhibits voltage-dependent potassium channels. Inhibits Kv1.3/KCNA3 potently and also blocks Kv1.1/KCNA1, Kv1.4/KCNA4, and Kv1.6/KCNA6 at subnanomolar concentrations.<ref>PMID:7660365</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bezanilla, F]] | + | [[Category: Stichodactyla helianthus]] |
| - | [[Category: Dang, B]] | + | [[Category: Bezanilla F]] |
| - | [[Category: Kent, S B.H]] | + | [[Category: Dang B]] |
| - | [[Category: Kubota, T]] | + | [[Category: Kent SBH]] |
| - | [[Category: Manda, K l]] | + | [[Category: Kubota T]] |
| - | [[Category: Roux, B]] | + | [[Category: Manda Kl]] |
| - | [[Category: Shen, R]] | + | [[Category: Roux B]] |
| - | [[Category: Allo-thr31-shk]]
| + | [[Category: Shen R]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
K1A_STIHL Inhibits voltage-dependent potassium channels. Inhibits Kv1.3/KCNA3 potently and also blocks Kv1.1/KCNA1, Kv1.4/KCNA4, and Kv1.6/KCNA6 at subnanomolar concentrations.[1]
Publication Abstract from PubMed
ShK toxin is a cysteine-rich 35-residue protein ion-channel ligand isolated from the sea anemone Stichodactyla helianthus. In this work, we studied the effect of inverting the side chain stereochemistry of individual Thr or Ile residues on the properties of the ShK protein. Molecular dynamics simulations were used to calculate the free energy cost of inverting the side-chain stereochemistry of individual Thr or Ile residues. Guided by the computational results, we used chemical protein synthesis to prepare three ShK polypeptide chain analogues, each containing either an allo-Thr or an allo-Ile residue. The three allo-Thr or allo-Ile-containing ShK polypeptides were able to fold into defined protein products, but with different folding propensities. Their relative thermal stabilities were measured and were consistent with the MD simulation data. Structures of the three ShK analogue proteins were determined by quasi-racemic X-ray crystallography and were similar to wild-type ShK. All three ShK analogues retained ion-channel blocking activity.
Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin.,Dang B, Shen R, Kubota T, Mandal K, Bezanilla F, Roux B, Kent SB Angew Chem Int Ed Engl. 2017 Feb 14. doi: 10.1002/anie.201612398. PMID:28194851[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Castaneda O, Sotolongo V, Amor AM, Stocklin R, Anderson AJ, Harvey AL, Engstrom A, Wernstedt C, Karlsson E. Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. Toxicon. 1995 May;33(5):603-13. PMID:7660365
- ↑ Dang B, Shen R, Kubota T, Mandal K, Bezanilla F, Roux B, Kent SB. Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 2017 Feb 14. doi: 10.1002/anie.201612398. PMID:28194851 doi:http://dx.doi.org/10.1002/anie.201612398
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