Structure and binding interface of the cytosolic tails of αXβ2 integrin.

<h4>Background</h4>Integrins are signal transducer proteins involved in a number of vital physiological processes including cell adhesion, proliferation and migration. Integrin molecules are hetero-dimers composed of two distinct subunits, α and β. In humans, 18 α and 8 β subunits are co...

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Autores principales:	Geok-Lin Chua, Xiao-Yan Tang, Alok Tanala Patra, Suet-Mien Tan, Surajit Bhattacharjya
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9be08ba3159942bc9379e14272690f2d
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spelling	oai:doaj.org-article:9be08ba3159942bc9379e14272690f2d2021-11-18T07:10:55ZStructure and binding interface of the cytosolic tails of αXβ2 integrin.1932-620310.1371/journal.pone.0041924https://doaj.org/article/9be08ba3159942bc9379e14272690f2d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22844534/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Integrins are signal transducer proteins involved in a number of vital physiological processes including cell adhesion, proliferation and migration. Integrin molecules are hetero-dimers composed of two distinct subunits, α and β. In humans, 18 α and 8 β subunits are combined into 24 different integrin molecules. Each of the subunit comprises a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). The CTs of integrins are vital for bidirectional signal transduction and in maintaining the resting state of the receptors. A large number of intracellular proteins have been found to interact with the CTs of integrins linking integrins to the cytoskeleton.<h4>Methodology/principal findings</h4>In this work, we have investigated structure and interactions of CTs of the leukocyte specific integrin αXβ2. We determined the atomic resolution structure of a myristoylated CT of αX in perdeuterated dodecylphosphocholine (DPC) by NMR spectroscopy. Our results reveal that the 35-residue long CT of αX adopts an α-helical conformation for residues F4-N17 at the N-terminal region. The remaining residues located at the C-terminal segment of αX delineate a long loop of irregular conformations. A segment of the loop maintains packing interactions with the helical structure by an extended non-polar surface of the αX CT. Interactions between αX and β2 CTs are demonstrated by (15)N-(1)H HSQC NMR experiments. We find that residues constituting the polar face of the helical conformation of αX are involved in interactions with the N-terminal residues of β2 CT. A docked structure of the CT complex indicates that a network of polar and/or salt-bridge interactions may sustain the heteromeric interactions.<h4>Conclusions/significance</h4>The current study provides important insights into the conservation of interactions and structures among different CTs of integrins.Geok-Lin ChuaXiao-Yan TangAlok Tanala PatraSuet-Mien TanSurajit BhattacharjyaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e41924 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Geok-Lin Chua Xiao-Yan Tang Alok Tanala Patra Suet-Mien Tan Surajit Bhattacharjya Structure and binding interface of the cytosolic tails of αXβ2 integrin.
description	<h4>Background</h4>Integrins are signal transducer proteins involved in a number of vital physiological processes including cell adhesion, proliferation and migration. Integrin molecules are hetero-dimers composed of two distinct subunits, α and β. In humans, 18 α and 8 β subunits are combined into 24 different integrin molecules. Each of the subunit comprises a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). The CTs of integrins are vital for bidirectional signal transduction and in maintaining the resting state of the receptors. A large number of intracellular proteins have been found to interact with the CTs of integrins linking integrins to the cytoskeleton.<h4>Methodology/principal findings</h4>In this work, we have investigated structure and interactions of CTs of the leukocyte specific integrin αXβ2. We determined the atomic resolution structure of a myristoylated CT of αX in perdeuterated dodecylphosphocholine (DPC) by NMR spectroscopy. Our results reveal that the 35-residue long CT of αX adopts an α-helical conformation for residues F4-N17 at the N-terminal region. The remaining residues located at the C-terminal segment of αX delineate a long loop of irregular conformations. A segment of the loop maintains packing interactions with the helical structure by an extended non-polar surface of the αX CT. Interactions between αX and β2 CTs are demonstrated by (15)N-(1)H HSQC NMR experiments. We find that residues constituting the polar face of the helical conformation of αX are involved in interactions with the N-terminal residues of β2 CT. A docked structure of the CT complex indicates that a network of polar and/or salt-bridge interactions may sustain the heteromeric interactions.<h4>Conclusions/significance</h4>The current study provides important insights into the conservation of interactions and structures among different CTs of integrins.
format	article
author	Geok-Lin Chua Xiao-Yan Tang Alok Tanala Patra Suet-Mien Tan Surajit Bhattacharjya
author_facet	Geok-Lin Chua Xiao-Yan Tang Alok Tanala Patra Suet-Mien Tan Surajit Bhattacharjya
author_sort	Geok-Lin Chua
title	Structure and binding interface of the cytosolic tails of αXβ2 integrin.
title_short	Structure and binding interface of the cytosolic tails of αXβ2 integrin.
title_full	Structure and binding interface of the cytosolic tails of αXβ2 integrin.
title_fullStr	Structure and binding interface of the cytosolic tails of αXβ2 integrin.
title_full_unstemmed	Structure and binding interface of the cytosolic tails of αXβ2 integrin.
title_sort	structure and binding interface of the cytosolic tails of αxβ2 integrin.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/9be08ba3159942bc9379e14272690f2d
work_keys_str_mv	AT geoklinchua structureandbindinginterfaceofthecytosolictailsofaxb2integrin AT xiaoyantang structureandbindinginterfaceofthecytosolictailsofaxb2integrin AT aloktanalapatra structureandbindinginterfaceofthecytosolictailsofaxb2integrin AT suetmientan structureandbindinginterfaceofthecytosolictailsofaxb2integrin AT surajitbhattacharjya structureandbindinginterfaceofthecytosolictailsofaxb2integrin
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Structure and binding interface of the cytosolic tails of αXβ2 integrin.

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