Document Detail

Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.
MedLine Citation:
PMID:  19361517     Owner:  NLM     Status:  MEDLINE    
Members of the ErbB/HER family of epidermal growth factor receptor tyrosine kinases cross a membrane with a single transmembrane (TM) helix. ErbB receptors form diverse homo- and heterodimers, which substantially increases the signaling potential of ErbB receptors. The involvement of the ErbB TM domains in homo- and heterodimerization is largely enigmatic. In this study, we experimentally analyzed the potential role of two conserved GxxxG-like motifs for mediating and/or stabilizing homo- and hetero-oligomeric interactions of the human ErbB TM domains. Both motifs appear to be critical for homo- and hetero-oligomeric TM helix interactions. Consequently, multiple TM structures are possible for the various ErbB homo- and heterodimers, which might be critical for the formation and TM signaling of specific ErbB pairs in vivo.
Claudia Escher; Florian Cymer; Dirk Schneider
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-04-08
Journal Detail:
Title:  Journal of molecular biology     Volume:  389     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-05-12     Completed Date:  2009-06-04     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  10-6     Citation Subset:  IM    
Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, Freiburg, Germany.
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MeSH Terms
Amino Acid Motifs
Amino Acid Sequence
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Multimerization*
Protein Structure, Tertiary
Receptor Protein-Tyrosine Kinases / chemistry*,  metabolism*
Structure-Activity Relationship
Reg. No./Substance:
EC Protein-Tyrosine Kinases

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