Mondal, Sukanta and Vijayan, Ramachandran and Shichina, Kannambath and Babu, Rajasekaran Mohan and Ramakumar, Suryanarayanarao (2005) I-Superfamily Conotoxins: Sequence and Structure Analysis. In: In Silico Biology, 5 (5-6). 557 - 571.
Full text not available from this repository. (Request a copy)Abstract
I-superfamily conotoxins have four-disulfide bonds with cysteine arrangement C-C-CC-CC-C-C, and they inhibit or modify ion channels of nerve cells. They have been characterized only recently and are relatively less well studied compared to other superfamily conotoxins. We have detected selective and sensitive sequence pattern for I-superfamily conotoxins. The availability of sequence pattern should be useful in protein family classification and functional annotation. We have built by homology modeling, a theoretical structural 3D model of ViTx from Conus virgo, a typical member of I-superfamily conotoxins. The modeling was based on the available 3D structure of Janus-atracotoxin-Hv1c of Janus-atracotoxin family whose members have been suggested as possible biopesticides. A study comparing the theoretically modeled structure of ViTx, with experimentally determined structures of other toxins, which share functional similarity with ViTx, reveals the crucial role of C-terminal region of ViTx in blocking therapeutically important voltage-gated potassium channels.
| Item Type: | Journal Article |
|---|---|
| Publication: | In Silico Biology |
| Publisher: | IOS Press |
| Additional Information: | The Copyright belongs to IOS Press. |
| Keywords: | I-superfamily conotoxins;protein sequence pattern;homology modeling;shaker K^+ channel;inhibitor cystine knot |
| Department/Centre: | Division of Information Sciences (Doesn't exist now) > BioInformatics Centre Division of Physical & Mathematical Sciences > Physics |
| Date Deposited: | 03 Apr 2006 |
| Last Modified: | 27 Aug 2008 11:51 |
| URI: | http://eprints.iisc.ac.in/id/eprint/6161 |
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