2giz: Difference between revisions

New page: left|200px<br /><applet load="2giz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2giz, resolution 1.68Å" /> '''Structural and funct...
 
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[[Image:2giz.gif|left|200px]]<br /><applet load="2giz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2giz.gif|left|200px]]<br /><applet load="2giz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2giz, resolution 1.68&Aring;" />
caption="2giz, resolution 1.68&Aring;" />
'''Structural and functional analysis of Natrin, a member of crisp-3 family blocks a variety of ion channels'''<br />
'''Structural and functional analysis of Natrin, a member of crisp-3 family blocks a variety of ion channels'''<br />


==Overview==
==Overview==
Cysteine-rich secretory proteins (CRISPs) are secreted single-chain, proteins found in different sources. Natrin is a member of the CRISP, family purified from the snake venom of Naja naja atra, which has been, reported as a BKca channel blocker. In our study, crystals of natrin were, obtained in two different crystal forms and the structure of one of them, was solved at a resolution of 1.68A. Our electrophysiological experiments, indicated that natrin can block the ion channel currents of the, voltage-gated potassium channel Kv1.3. Docking analyses of the interaction, between natrin and Kv1.3 revealed a novel interaction pattern different, from the two previously reported K(+) channel inhibition models termed, "functional dyad" and "basic ring". These findings offered new insights, into the function of natrin and how the specific interactions between, CRISPs and different ion channels can be achieved.
Cysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our study, crystals of natrin were obtained in two different crystal forms and the structure of one of them was solved at a resolution of 1.68A. Our electrophysiological experiments indicated that natrin can block the ion channel currents of the voltage-gated potassium channel Kv1.3. Docking analyses of the interaction between natrin and Kv1.3 revealed a novel interaction pattern different from the two previously reported K(+) channel inhibition models termed "functional dyad" and "basic ring". These findings offered new insights into the function of natrin and how the specific interactions between CRISPs and different ion channels can be achieved.


==About this Structure==
==About this Structure==
2GIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GIZ OCA].  
2GIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GIZ OCA].  


==Reference==
==Reference==
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[[Category: electrophysiology]]
[[Category: electrophysiology]]


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