1yl2
From Proteopedia
(New page: 200px<br /><applet load="1yl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yl2" /> '''Conkunitzin-S1 is the first member of a new ...) |
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| - | [[Image:1yl2.jpg|left|200px]]<br /><applet load="1yl2" size=" | + | [[Image:1yl2.jpg|left|200px]]<br /><applet load="1yl2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yl2" /> | caption="1yl2" /> | ||
'''Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family- Structural and functional characterization'''<br /> | '''Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family- Structural and functional characterization'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Conkunitzin-S1 (Conk-S1) is a 60-residue neurotoxin from the venom of the | + | Conkunitzin-S1 (Conk-S1) is a 60-residue neurotoxin from the venom of the cone snail Conus striatus that interacts with voltage-gated potassium channels. Conk-S1 shares sequence homology with Kunitz-type proteins but contains only two out of the three highly conserved cysteine bridges, which are typically found in these small, basic protein modules. In this study the three-dimensional structure of Conk-S1 has been solved by multidimensional NMR spectroscopy. The solution structure of recombinant Conk-S1 shows that a Kunitz fold is present, even though one of the highly conserved disulfide cross-links is missing. Introduction of a third, homologous disulfide bond into Conk-S1 results in a functional toxin with similar affinity for Shaker potassium channels. The affinity of Conk-S1 can be enhanced by a pore mutation within the Shaker channel pore indicating an interaction of Conk-S1 with the vestibule of potassium channels. |
==About this Structure== | ==About this Structure== | ||
| - | 1YL2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full crystallographic information is available from [http:// | + | 1YL2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YL2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Graf, R.]] | [[Category: Graf, R.]] | ||
[[Category: Korukottu, J.]] | [[Category: Korukottu, J.]] | ||
| - | [[Category: Olivera, B | + | [[Category: Olivera, B M.]] |
[[Category: Terlau, H.]] | [[Category: Terlau, H.]] | ||
[[Category: Vijayan, V.]] | [[Category: Vijayan, V.]] | ||
| Line 24: | Line 24: | ||
[[Category: neurotoxin; kunitz-domain; potassium channel blocker]] | [[Category: neurotoxin; kunitz-domain; potassium channel blocker]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:28 2008'' |
Revision as of 14:06, 21 February 2008
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Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family- Structural and functional characterization
Overview
Conkunitzin-S1 (Conk-S1) is a 60-residue neurotoxin from the venom of the cone snail Conus striatus that interacts with voltage-gated potassium channels. Conk-S1 shares sequence homology with Kunitz-type proteins but contains only two out of the three highly conserved cysteine bridges, which are typically found in these small, basic protein modules. In this study the three-dimensional structure of Conk-S1 has been solved by multidimensional NMR spectroscopy. The solution structure of recombinant Conk-S1 shows that a Kunitz fold is present, even though one of the highly conserved disulfide cross-links is missing. Introduction of a third, homologous disulfide bond into Conk-S1 results in a functional toxin with similar affinity for Shaker potassium channels. The affinity of Conk-S1 can be enhanced by a pore mutation within the Shaker channel pore indicating an interaction of Conk-S1 with the vestibule of potassium channels.
About this Structure
1YL2 is a Protein complex structure of sequences from Conus striatus. Full crystallographic information is available from OCA.
Reference
Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization., Bayrhuber M, Vijayan V, Ferber M, Graf R, Korukottu J, Imperial J, Garrett JE, Olivera BM, Terlau H, Zweckstetter M, Becker S, J Biol Chem. 2005 Jun 24;280(25):23766-70. Epub 2005 Apr 15. PMID:15833744
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