Mondal, Sukanta and Rajasekaran, Mohan B and Rajasekaran, Bhavna and Ramakumar, Suryanarayanarao (2006) I-conotoxin superfamily revisited. In: Journal of Peptide Science, 12 (11). 679- 685.
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The I-conotoxin superfamily (I-Ctx) is known to have four disulfide bonds with the cysteine arrangement C-C-CC-CC-C-C, and the members inhibit or modify ion channels of nerve cells. Recently, Olivera and co-workers (FEBS J. 2005; 272: 4178-4188) have suggested that the previously described I-Ctx should now be divided into two different gene superfamilies, namely, $I_1$ and $I_2$, in view of their having two different types of signal peptides and exhibiting distinct functions. We have revisited the 28 entries presently grouped as I-Ctx in UniProt Swiss-Prot knowledgebase, and on the basis of in silico analysis have divided them into $I_1$ and $I_2$ superfamilies. The sequence analysis has provided a framework for in silico annotation enabling us to carry out computer-based functional characterization of the UniProtKB/TrEMBL entry Q59AA4 from Conus miles and to predict it as a member of the $I_2$ superfamily. Furthermore, we have predicted the mature toxin of this entry and have proposed that it may be an inhibitor of voltage-gated potassium channels.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley and Sons.|
|Keywords:||Signal peptide;Mature toxin;Gene superfamily;Potassium channel inhibitor;Functional annotation|
|Department/Centre:||Division of Information Sciences > BioInformatics Centre
Division of Physical & Mathematical Sciences > Physics
|Date Deposited:||13 May 2008|
|Last Modified:||19 Sep 2010 04:44|
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