Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction

Disintegrins are small cysteine-rich proteins found in a variety of snake venom. These proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell and cell-matrix interaction that are widely studied as therapeutic targets. Snake venom disintegrins emerged from the...

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Autores principales:	Ariana A. Vasconcelos, Jorge C. Estrada, Victor David, Luciana S. Wermelinger, Fabio C. L. Almeida, Russolina B. Zingali
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	snake venom disintegrin structure integrin NMR crystallography Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/070e4d89500c4200a16f6a897ef11ad2
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spelling	oai:doaj.org-article:070e4d89500c4200a16f6a897ef11ad22021-12-03T06:39:16ZStructure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction2296-889X10.3389/fmolb.2021.783301https://doaj.org/article/070e4d89500c4200a16f6a897ef11ad22021-12-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmolb.2021.783301/fullhttps://doaj.org/toc/2296-889XDisintegrins are small cysteine-rich proteins found in a variety of snake venom. These proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell and cell-matrix interaction that are widely studied as therapeutic targets. Snake venom disintegrins emerged from the snake venom metalloproteinase and are classified according to the sequence size and number of disulfide bonds. Evolutive structure and function diversification of disintegrin family involves a stepwise decrease in the polypeptide chain, loss of cysteine residues, and selectivity. Since the structure elucidation of echistatin, the description of the structural properties of disintegrins has allowed the investigation of the mechanisms involved in integrin-cell-extracellular matrix interaction. This review provides an analysis of the structures of all family groups enabling the description of an expanded classification of the disintegrin family in seven groups. Each group presents a particular disulfide pattern and sequence signatures, facilitating the identification of new disintegrins. The classification was based on the disintegrin-like domain of the human metalloproteinase (ADAM-10). We also present the sequence and structural signatures important for disintegrin-integrin interaction, unveiling the relationship between the structure and function of these proteins.Ariana A. VasconcelosAriana A. VasconcelosJorge C. EstradaVictor DavidLuciana S. WermelingerFabio C. L. AlmeidaFabio C. L. AlmeidaRussolina B. ZingaliFrontiers Media S.A.articlesnake venom disintegrinstructureintegrinNMRcrystallographyBiology (General)QH301-705.5ENFrontiers in Molecular Biosciences, Vol 8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	snake venom disintegrin structure integrin NMR crystallography Biology (General) QH301-705.5
spellingShingle	snake venom disintegrin structure integrin NMR crystallography Biology (General) QH301-705.5 Ariana A. Vasconcelos Ariana A. Vasconcelos Jorge C. Estrada Victor David Luciana S. Wermelinger Fabio C. L. Almeida Fabio C. L. Almeida Russolina B. Zingali Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
description	Disintegrins are small cysteine-rich proteins found in a variety of snake venom. These proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell and cell-matrix interaction that are widely studied as therapeutic targets. Snake venom disintegrins emerged from the snake venom metalloproteinase and are classified according to the sequence size and number of disulfide bonds. Evolutive structure and function diversification of disintegrin family involves a stepwise decrease in the polypeptide chain, loss of cysteine residues, and selectivity. Since the structure elucidation of echistatin, the description of the structural properties of disintegrins has allowed the investigation of the mechanisms involved in integrin-cell-extracellular matrix interaction. This review provides an analysis of the structures of all family groups enabling the description of an expanded classification of the disintegrin family in seven groups. Each group presents a particular disulfide pattern and sequence signatures, facilitating the identification of new disintegrins. The classification was based on the disintegrin-like domain of the human metalloproteinase (ADAM-10). We also present the sequence and structural signatures important for disintegrin-integrin interaction, unveiling the relationship between the structure and function of these proteins.
format	article
author	Ariana A. Vasconcelos Ariana A. Vasconcelos Jorge C. Estrada Victor David Luciana S. Wermelinger Fabio C. L. Almeida Fabio C. L. Almeida Russolina B. Zingali
author_facet	Ariana A. Vasconcelos Ariana A. Vasconcelos Jorge C. Estrada Victor David Luciana S. Wermelinger Fabio C. L. Almeida Fabio C. L. Almeida Russolina B. Zingali
author_sort	Ariana A. Vasconcelos
title	Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
title_short	Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
title_full	Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
title_fullStr	Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
title_full_unstemmed	Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction
title_sort	structure-function relationship of the disintegrin family: sequence signature and integrin interaction
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/070e4d89500c4200a16f6a897ef11ad2
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Structure-Function Relationship of the Disintegrin Family: Sequence Signature and Integrin Interaction

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