2ca7

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(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="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ca7.gif|left|200px]]<br /><applet load="2ca7" size="350" color="white" frame="true" align="right" spinBox="true"
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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CA7 OCA].
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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]]
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[[Category: Garrett, J.E.]]
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[[Category: Garrett, J E.]]
[[Category: Graf, R.]]
[[Category: Graf, R.]]
[[Category: Imperial, J.]]
[[Category: Imperial, J.]]
[[Category: Korukottu, J.]]
[[Category: Korukottu, J.]]
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[[Category: Olivera, B.M.]]
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[[Category: Olivera, B M.]]
[[Category: Terlau, H.]]
[[Category: Terlau, H.]]
[[Category: Vijayan, V.]]
[[Category: Vijayan, V.]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:03:39 2007''
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''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

Image:2ca7.gif

2ca7

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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

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