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I‐conotoxin superfamily revisited
Author(s) -
Mondal Sukanta,
Babu Rajasekaran Mohan,
Bhavna Rajasekaran,
Ramakumar Suryanarayanarao
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.778
Subject(s) - conotoxin , uniprot , in silico , superfamily , computational biology , biology , cysteine , protein sequencing , sequence analysis , biochemistry , peptide sequence , gene , peptide , enzyme
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. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.