Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.

Snake venoms are rich sources of biologically active proteins and polypeptides. Three-finger toxins are non-enzymatic proteins present in elapid (cobras, kraits, mambas and sea snakes) and colubrid venoms. These proteins contain four conserved disulfide bonds in the core to maintain the three-finger...

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Autores principales:	Vallerinteavide Mavelli Girish, Sundramurthy Kumar, Lissa Joseph, Chacko Jobichen, R Manjunatha Kini, J Sivaraman
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a20ba1de11b14750a8565f9ed765b79f
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spelling	oai:doaj.org-article:a20ba1de11b14750a8565f9ed765b79f2021-11-18T08:10:45ZIdentification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.1932-620310.1371/journal.pone.0048112https://doaj.org/article/a20ba1de11b14750a8565f9ed765b79f2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23144733/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Snake venoms are rich sources of biologically active proteins and polypeptides. Three-finger toxins are non-enzymatic proteins present in elapid (cobras, kraits, mambas and sea snakes) and colubrid venoms. These proteins contain four conserved disulfide bonds in the core to maintain the three-finger folds. Although all three-finger toxins have similar fold, their biological activities are different. A new three-finger toxin (hemachatoxin) was isolated from Hemachatus haemachatus (Ringhals cobra) venom. Its amino acid sequence was elucidated, and crystal structure was determined at 2.43 Å resolution. The overall fold is similar to other three-finger toxins. The structure and sequence analysis revealed that the fold is maintained by four highly conserved disulfide bonds. It exhibited highest similarity to particularly P-type cardiotoxins that are known to associate and perturb the membrane surface with their lipid binding sites. Also, the increased B value of hemachotoxin loop II suggests that loop II is flexible and may remain flexible until its interaction with membrane phospholipids. Based on the analysis, we predict hemachatoxin to be cardiotoxic/cytotoxic and our future experiments will be directed to characterize the activity of hemachatoxin.Vallerinteavide Mavelli GirishSundramurthy KumarLissa JosephChacko JobichenR Manjunatha KiniJ SivaramanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e48112 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Vallerinteavide Mavelli Girish Sundramurthy Kumar Lissa Joseph Chacko Jobichen R Manjunatha Kini J Sivaraman Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
description	Snake venoms are rich sources of biologically active proteins and polypeptides. Three-finger toxins are non-enzymatic proteins present in elapid (cobras, kraits, mambas and sea snakes) and colubrid venoms. These proteins contain four conserved disulfide bonds in the core to maintain the three-finger folds. Although all three-finger toxins have similar fold, their biological activities are different. A new three-finger toxin (hemachatoxin) was isolated from Hemachatus haemachatus (Ringhals cobra) venom. Its amino acid sequence was elucidated, and crystal structure was determined at 2.43 Å resolution. The overall fold is similar to other three-finger toxins. The structure and sequence analysis revealed that the fold is maintained by four highly conserved disulfide bonds. It exhibited highest similarity to particularly P-type cardiotoxins that are known to associate and perturb the membrane surface with their lipid binding sites. Also, the increased B value of hemachotoxin loop II suggests that loop II is flexible and may remain flexible until its interaction with membrane phospholipids. Based on the analysis, we predict hemachatoxin to be cardiotoxic/cytotoxic and our future experiments will be directed to characterize the activity of hemachatoxin.
format	article
author	Vallerinteavide Mavelli Girish Sundramurthy Kumar Lissa Joseph Chacko Jobichen R Manjunatha Kini J Sivaraman
author_facet	Vallerinteavide Mavelli Girish Sundramurthy Kumar Lissa Joseph Chacko Jobichen R Manjunatha Kini J Sivaraman
author_sort	Vallerinteavide Mavelli Girish
title	Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
title_short	Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
title_full	Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
title_fullStr	Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
title_full_unstemmed	Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.
title_sort	identification and structural characterization of a new three-finger toxin hemachatoxin from hemachatus haemachatus venom.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/a20ba1de11b14750a8565f9ed765b79f
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Identification and structural characterization of a new three-finger toxin hemachatoxin from Hemachatus haemachatus venom.

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