A Bilwes

A McCoy

A Ricciardi

A Roy

Alejandra Bravo

AV Osipov

B Rees

C Fruchart-Gaillard

C Rouget

CD Dellisanti

CH Wang

Chacko Jobichen

CM Fletcher

D Kordis

D Servent

DV Dementieva

E Karlsson

F Forouhar

F Nau

F Teixeira-Clerc

FJ Joubert

GA Grant

HV Kolbe

IL Junqueira-de-Azevedo

J Eastman

J Fernández

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JA Rosenthal

JC Dewan

JF Gaucher

JM Carsi

JP Albrand

JS Joseph

KH Ruan

KY Chien

L Fryklund

L Holm

L Quinton

Lissa Joseph

LM Colquhoun

M Harel

M Larkin

M Ohno

M Ploug

MH le Du

MJ Dufton

MJ Sutcliffe

N Rajagopalan

O Yasuda

P Emsley

P Gouet

PD Adams

PL Wu

PV Dubovskii

PW Corfield

R Laskowski

R. Manjunatha Kini

RA Love

RE Oswald

RJ Lewis

RM Kini

RS McDowell

S Altschul

S Antil

S Antil-Delbeke

S Nirthanan

S Pahari

SC Lee

Sundramurthy Kumar

T Ogawa

TP Gumley

TS Chen

TS Kang

V Tsetlin

V Zupunski

Vallerinteavide Mavelli Girish

WeilleJR de

X Hou

Y Bourne

YJ Sun

PLoS ONE

PubMed

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

Girish, Vallerinteavide Mavelli

Kumar, Sundramurthy

Joseph, Lissa

Jobichen, Chacko

Kini, R. Manjunatha

Sivaraman, J.

VCU Scholars Compass

Identification and Structural Characterization of a New Three-Finger Toxin Hemachatoxin from Hemachatus haemachatus Venom

Girish Vallerinteavide Mavelli

Kumar Sundramurthy

Joseph Lissa

Jobichen Chacko

Kini R. Manjunatha

Sivaraman J.

Public Library of Science (PLOS)

 Venom

R Manjunatha Kini

J Sivaraman

Directory of Open Access Journals

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 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 A ̊ 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 wil

CiteSeerX

<div><p>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 <em>Hemachatus haemachatus</em> (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.</p> </div

Vallerinteavide Mavelli Girish (124794)

Sundramurthy Kumar (124796)

Lissa Joseph (124797)

Chacko Jobichen (43238)

R. Manjunatha Kini (124799)

J. Sivaraman (31440)

The Francis Crick Institute

Identification and Structural Characterization of a New Three-Finger Toxin Hemachatoxin from <em>Hemachatus haemachatus</em> Venom

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Identification and Structural Characterization of a New Three-Finger Toxin Hemachatoxin from Hemachatus haemachatus Venom

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