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2ca7
From Proteopedia
(New page: 200px<br /><applet load="2ca7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ca7" /> '''CONKUNITZIN-S1 IS THE FIRST MEMBER OF A NEW ...) |
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| - | [[Image:2ca7.gif|left|200px]]<br /><applet load="2ca7" size=" | + | [[Image:2ca7.gif|left|200px]]<br /><applet load="2ca7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ca7" /> | caption="2ca7" /> | ||
'''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== | ||
| - | 2CA7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full crystallographic information is available from [http:// | + | 2CA7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2CA7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Becker, S.]] | [[Category: Becker, S.]] | ||
[[Category: Ferber, M]] | [[Category: Ferber, M]] | ||
| - | [[Category: Garrett, J | + | [[Category: Garrett, J E.]] |
[[Category: Graf, R.]] | [[Category: Graf, R.]] | ||
[[Category: Imperial, J.]] | [[Category: Imperial, J.]] | ||
[[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 31: | Line 31: | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:36 2008'' |
Revision as of 14:46, 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
2CA7 is a Single protein structure of sequence 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
Page seeded by OCA on Thu Feb 21 16:46:36 2008
Categories: Conus striatus | Single protein | Bayrhuber, M. | Becker, S. | Ferber, M | Garrett, J E. | Graf, R. | Imperial, J. | Korukottu, J. | Olivera, B M. | Terlau, H. | Vijayan, V. | Zweckstetter, M. | Conkunitzin | Kunitz-domain | Kunitz-type fold | Neurotoxin | Potassium channel inhibitor | Toxin
