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Snake Venom Metalloproteinases (SVMPs): A structure-function update

Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition of platelet aggregation. Due to these activit...

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Autores principales: Olaoba, Olamide Tosin, Karina dos Santos, Patty, Selistre-de-Araujo, Heloisa Sobreiro, Ferreira de Souza, Dulce Helena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7399193/
https://www.ncbi.nlm.nih.gov/pubmed/32776002
http://dx.doi.org/10.1016/j.toxcx.2020.100052
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author Olaoba, Olamide Tosin
Karina dos Santos, Patty
Selistre-de-Araujo, Heloisa Sobreiro
Ferreira de Souza, Dulce Helena
author_facet Olaoba, Olamide Tosin
Karina dos Santos, Patty
Selistre-de-Araujo, Heloisa Sobreiro
Ferreira de Souza, Dulce Helena
author_sort Olaoba, Olamide Tosin
collection PubMed
description Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition of platelet aggregation. Due to these activities, SVMPs are responsible for many of the well-known pathological phenotypes in snake envenomations caused particularly by species from the Viperidae family and the Crotalinae subfamily. These proteins have been classified based on their size and domain structure into P–I, P-II and P-III classes. Comparatively, members of the P–I SVMPs possess the simplest structures, formed by the catalytic metalloproteinase domain only; the P-II SVMPs are moderately more complex, having the canonical disintegrin domain in addition to the metalloproteinase domain; members of the P-III class are more structurally varied, comprising the metalloproteinase, disintegrin-like, and cysteine-rich domains. Proteolytic cleavage, repeated domain loss and presence of other ancillary domains are responsible for structural diversities in the P-III class. However, studies continue to unveil the relationship between the structure and function of these proteins. In this review, we recovered evidences from literature on the structural peculiarities and functional classification of Snake Venom Metalloproteinases. In addition, we reflect on diversities that exist among each class while taking into account specific and up-to-date class-based activities.
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spelling pubmed-73991932020-08-06 Snake Venom Metalloproteinases (SVMPs): A structure-function update Olaoba, Olamide Tosin Karina dos Santos, Patty Selistre-de-Araujo, Heloisa Sobreiro Ferreira de Souza, Dulce Helena Toxicon X Venomics at the crossroads between ecological and clinical toxinology, Edited by: Dr. Juan Calvete, Dr.Jose Maria Gutiérrez and Dr. Cleópatra A.S. Caldeira Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition of platelet aggregation. Due to these activities, SVMPs are responsible for many of the well-known pathological phenotypes in snake envenomations caused particularly by species from the Viperidae family and the Crotalinae subfamily. These proteins have been classified based on their size and domain structure into P–I, P-II and P-III classes. Comparatively, members of the P–I SVMPs possess the simplest structures, formed by the catalytic metalloproteinase domain only; the P-II SVMPs are moderately more complex, having the canonical disintegrin domain in addition to the metalloproteinase domain; members of the P-III class are more structurally varied, comprising the metalloproteinase, disintegrin-like, and cysteine-rich domains. Proteolytic cleavage, repeated domain loss and presence of other ancillary domains are responsible for structural diversities in the P-III class. However, studies continue to unveil the relationship between the structure and function of these proteins. In this review, we recovered evidences from literature on the structural peculiarities and functional classification of Snake Venom Metalloproteinases. In addition, we reflect on diversities that exist among each class while taking into account specific and up-to-date class-based activities. Elsevier 2020-07-21 /pmc/articles/PMC7399193/ /pubmed/32776002 http://dx.doi.org/10.1016/j.toxcx.2020.100052 Text en © 2020 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Venomics at the crossroads between ecological and clinical toxinology, Edited by: Dr. Juan Calvete, Dr.Jose Maria Gutiérrez and Dr. Cleópatra A.S. Caldeira
Olaoba, Olamide Tosin
Karina dos Santos, Patty
Selistre-de-Araujo, Heloisa Sobreiro
Ferreira de Souza, Dulce Helena
Snake Venom Metalloproteinases (SVMPs): A structure-function update
title Snake Venom Metalloproteinases (SVMPs): A structure-function update
title_full Snake Venom Metalloproteinases (SVMPs): A structure-function update
title_fullStr Snake Venom Metalloproteinases (SVMPs): A structure-function update
title_full_unstemmed Snake Venom Metalloproteinases (SVMPs): A structure-function update
title_short Snake Venom Metalloproteinases (SVMPs): A structure-function update
title_sort snake venom metalloproteinases (svmps): a structure-function update
topic Venomics at the crossroads between ecological and clinical toxinology, Edited by: Dr. Juan Calvete, Dr.Jose Maria Gutiérrez and Dr. Cleópatra A.S. Caldeira
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7399193/
https://www.ncbi.nlm.nih.gov/pubmed/32776002
http://dx.doi.org/10.1016/j.toxcx.2020.100052
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