Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.

Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin...

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Autores principales:	Chaohua Lai, Xiaoxi Liu, Changlin Tian, Fangming Wu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bc1c1bdf56ae4284bf6d717ea6115677
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spelling	oai:doaj.org-article:bc1c1bdf56ae4284bf6d717ea61156772021-11-18T07:47:21ZIntegrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.1932-620310.1371/journal.pone.0062954https://doaj.org/article/bc1c1bdf56ae4284bf6d717ea61156772013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23646163/?tool=EBIhttps://doaj.org/toc/1932-6203Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin α1 and β1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of α1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in α1-TMC. Structural comparisons of α1-TMC with reported αIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between α1-TMC and β1-TMC through several α1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.Chaohua LaiXiaoxi LiuChanglin TianFangming WuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e62954 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chaohua Lai Xiaoxi Liu Changlin Tian Fangming Wu Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
description	Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin α1 and β1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of α1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in α1-TMC. Structural comparisons of α1-TMC with reported αIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between α1-TMC and β1-TMC through several α1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.
format	article
author	Chaohua Lai Xiaoxi Liu Changlin Tian Fangming Wu
author_facet	Chaohua Lai Xiaoxi Liu Changlin Tian Fangming Wu
author_sort	Chaohua Lai
title	Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
title_short	Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
title_full	Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
title_fullStr	Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
title_full_unstemmed	Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
title_sort	integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/bc1c1bdf56ae4284bf6d717ea6115677
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Integrin α1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.

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