Linked Life Data

17042488

Source:http://linkedlifedata.com/resource/pubmed/id/17042488

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pubmed-article:17042488pubmed:abstractTextThe transmembrane (TM) and juxtamembrane (JM) regions of the epidermal growth factor receptor (EGFR) couple ligand binding in the extracellular domain to activation of the kinase domain. Solid-state NMR and polarized FTIR measurements of peptides corresponding to the TM plus JM regions of EGFR (residues 622-660) reconstituted in model phospholipid membranes are presented to address the role of the short cytoplasmic JM sequence (residues 645-660) in regulating EGFR activity. We show that the TM domain is helical with a transition to non-helical structure at the TM-JM boundary. Fluorescence measurements indicate that the JM region of EGFR(622-660) binds to the membrane surface and that binding can be reversed by the addition of the complex of Ca2+ and calmodulin. Together these data support models suggesting the cytoplasmic JM region of EGFR plays an active role in regulating receptor activity.lld:pubmed
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pubmed-article:17042488pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:17042488pubmed:articleTitleStructure of the membrane reconstituted transmembrane-juxtamembrane peptide EGFR(622-660) and its interaction with Ca2+/calmodulin.lld:pubmed
pubmed-article:17042488pubmed:affiliationDepartment of Biochemistry and Cell Biology, Center for Structural Biology, Stony Brook University, Stony Brook, New York 11794-5215, USA.lld:pubmed
pubmed-article:17042488pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17042488pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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pubmed-article:17042488pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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