Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom

Detalhes bibliográficos
Autor(a) principal: Murakami, Mário T. [UNESP]
Data de Publicação: 2006
Outros Autores: Melo, Cristiane C. [UNESP], Angulo, Yamileth, Lomonte, Bruno, Arni, Raghuvir K. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1107/S1744309106010700
http://www.ncbi.nlm.nih.gov/pubmed/16682766
http://hdl.handle.net/11449/68864
Resumo: Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.
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spelling Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venomAtropoides nummifermyotoxin II, Atropoides nummiferphospholipase Asnake venomamino acid sequencebinding sitechemistrycrystallizationmolecular geneticssequence alignmentX ray crystallographyAmino Acid SequenceBinding SitesCrotalid VenomsCrystallizationCrystallography, X-RayMolecular Sequence DataPhospholipases ASequence AlignmentLys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.Department of Physics IBILCE/UNESP, Sao Jose do Rio Preto-SPInstituto Clodomiro Picado Facultad de Microbiologia, San JoséDepartamento de Bioqúmica Escuela de Medicina Universidad de Costa Rica, San JoséCenter for Applied Toxinology Butantan Institute, São Paulo-SPDepartment of Physics IBILCE/UNESP, Sao Jose do Rio Preto-SPUniversidade Estadual Paulista (Unesp)Facultad de MicrobiologiaUniversidad de Costa RicaInstituto ButantanMurakami, Mário T. [UNESP]Melo, Cristiane C. [UNESP]Angulo, YamilethLomonte, BrunoArni, Raghuvir K. [UNESP]2014-05-27T11:21:51Z2014-05-27T11:21:51Z2006-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article423-426application/pdfhttp://dx.doi.org/10.1107/S1744309106010700http://www.ncbi.nlm.nih.gov/pubmed/16682766Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.1744-3091http://hdl.handle.net/11449/6886410.1107/S1744309106010700http://www.ncbi.nlm.nih.gov/pubmed/16682766WOS:0002371590000012-s2.0-33646836252WOS000237159000001.pdf91625089789458870000-0003-2460-1145Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengActa Crystallographica Section F: Structural Biology and Crystallization Communicationsinfo:eu-repo/semantics/openAccess2024-01-15T06:20:50Zoai:repositorio.unesp.br:11449/68864Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:02:59.287630Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
title Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
spellingShingle Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
Murakami, Mário T. [UNESP]
Atropoides nummifer
myotoxin II, Atropoides nummifer
phospholipase A
snake venom
amino acid sequence
binding site
chemistry
crystallization
molecular genetics
sequence alignment
X ray crystallography
Amino Acid Sequence
Binding Sites
Crotalid Venoms
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Phospholipases A
Sequence Alignment
title_short Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
title_full Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
title_fullStr Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
title_full_unstemmed Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
title_sort Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
author Murakami, Mário T. [UNESP]
author_facet Murakami, Mário T. [UNESP]
Melo, Cristiane C. [UNESP]
Angulo, Yamileth
Lomonte, Bruno
Arni, Raghuvir K. [UNESP]
author_role author
author2 Melo, Cristiane C. [UNESP]
Angulo, Yamileth
Lomonte, Bruno
Arni, Raghuvir K. [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Facultad de Microbiologia
Universidad de Costa Rica
Instituto Butantan
dc.contributor.author.fl_str_mv Murakami, Mário T. [UNESP]
Melo, Cristiane C. [UNESP]
Angulo, Yamileth
Lomonte, Bruno
Arni, Raghuvir K. [UNESP]
dc.subject.por.fl_str_mv Atropoides nummifer
myotoxin II, Atropoides nummifer
phospholipase A
snake venom
amino acid sequence
binding site
chemistry
crystallization
molecular genetics
sequence alignment
X ray crystallography
Amino Acid Sequence
Binding Sites
Crotalid Venoms
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Phospholipases A
Sequence Alignment
topic Atropoides nummifer
myotoxin II, Atropoides nummifer
phospholipase A
snake venom
amino acid sequence
binding site
chemistry
crystallization
molecular genetics
sequence alignment
X ray crystallography
Amino Acid Sequence
Binding Sites
Crotalid Venoms
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Phospholipases A
Sequence Alignment
description Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.
publishDate 2006
dc.date.none.fl_str_mv 2006-05-01
2014-05-27T11:21:51Z
2014-05-27T11:21:51Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1107/S1744309106010700
http://www.ncbi.nlm.nih.gov/pubmed/16682766
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.
1744-3091
http://hdl.handle.net/11449/68864
10.1107/S1744309106010700
http://www.ncbi.nlm.nih.gov/pubmed/16682766
WOS:000237159000001
2-s2.0-33646836252
WOS000237159000001.pdf
9162508978945887
0000-0003-2460-1145
url http://dx.doi.org/10.1107/S1744309106010700
http://www.ncbi.nlm.nih.gov/pubmed/16682766
http://hdl.handle.net/11449/68864
identifier_str_mv Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.
1744-3091
10.1107/S1744309106010700
WOS:000237159000001
2-s2.0-33646836252
WOS000237159000001.pdf
9162508978945887
0000-0003-2460-1145
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Acta Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 423-426
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808129484623183872

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