Carboxyl group footprinting mass spectrometry and molecular dynamics identify key interactions in the HER2-HER3 receptor tyrosine kinase interface

Timothy S. Collier, Karthikeyan Diraviyam, John Monsey, Wei Shen, David Sept, Ron Bose

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

Background: HER2 and HER3 receptor tyrosine kinases form potent oncogenic signaling dimers. Results: Carboxyl group footprinting and molecular dynamics reveal changes in the HER2-HER3 dimer interface and the HER2 activation loop. Conclusion: HER2 and HER3 form asymmetric heterodimers in a single configuration. The HER2 unphosphorylated activation loop can assume an active conformation. Significance: This study provides the first structural characterization of HER2-HER3 kinase dimers.

Original languageEnglish
Pages (from-to)25254-25264
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number35
DOIs
StatePublished - Aug 30 2013

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