PMID- 20471394
OWN - NLM
STAT- MEDLINE
DCOM- 20100628
LR  - 20181201
IS  - 1089-8638 (Electronic)
IS  - 0022-2836 (Linking)
VI  - 400
IP  - 2
DP  - 2010 Jul 9
TI  - Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 
      receptor tyrosine kinases.
PG  - 231-43
LID - 10.1016/j.jmb.2010.05.016 [doi]
AB  - Growth factor receptor tyrosine kinases of the ErbB family play a significant 
      role in vital cellular processes and various cancers. During signal transduction 
      across plasma membrane, ErbB receptors are involved in lateral homodimerization 
      and heterodimerization with proper assembly of their extracellular single-span 
      transmembrane (TM) and cytoplasmic domains. The ErbB1/ErbB2 heterodimer appears 
      to be the strongest and most potent inducer of cellular transformation and 
      mitogenic signaling compared to other ErbB homodimers and heterodimers. Spatial 
      structure of the heterodimeric complex formed by TM domains of ErbB1 and ErbB2 
      receptors embedded into lipid bicelles was obtained by solution NMR. The ErbB1 
      and ErbB2 TM domains associate in a right-handed alpha-helical bundle through 
      their N-terminal double GG4-like motif T(648)G(649)X(2)G(652)A(653) and glycine 
      zipper motif T(652)X(3)S(656)X(3)G(660), respectively. The described heterodimer 
      conformation is believed to support the juxtamembrane and kinase domain 
      configuration corresponding to the receptor active state. The capability for 
      multiple polar interactions, along with hydrogen bonding between TM segments, 
      correlates with the observed highest affinity of the ErbB1/ErbB2 heterodimer, 
      implying an important contribution of the TM helix-helix interaction to signal 
      transduction.
CI  - Copyright (c) 2010 Elsevier Ltd. All rights reserved.
FAU - Mineev, Konstantin S
AU  - Mineev KS
AD  - Division of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic 
      Chemistry RAS, ul. Miklukho-Maklaya, 16/10, Moscow 117997, Russia.
FAU - Bocharov, Eduard V
AU  - Bocharov EV
FAU - Pustovalova, Yulia E
AU  - Pustovalova YE
FAU - Bocharova, Olga V
AU  - Bocharova OV
FAU - Chupin, Vladimir V
AU  - Chupin VV
FAU - Arseniev, Alexander S
AU  - Arseniev AS
LA  - eng
SI  - PDB/2KS1
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100513
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Lipid Bilayers)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.10.1 (Receptor, ErbB-2)
SB  - IM
MH  - Amino Acid Sequence
MH  - ErbB Receptors/*chemistry/genetics/metabolism
MH  - Humans
MH  - Hydrogen Bonding
MH  - Lipid Bilayers/chemistry/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Protein Multimerization
MH  - *Protein Structure, Quaternary
MH  - *Protein Structure, Tertiary
MH  - Receptor, ErbB-2/*chemistry/genetics/metabolism
EDAT- 2010/05/18 06:00
MHDA- 2010/06/29 06:00
CRDT- 2010/05/18 06:00
PHST- 2010/01/05 00:00 [received]
PHST- 2010/04/25 00:00 [revised]
PHST- 2010/05/07 00:00 [accepted]
PHST- 2010/05/18 06:00 [entrez]
PHST- 2010/05/18 06:00 [pubmed]
PHST- 2010/06/29 06:00 [medline]
AID - S0022-2836(10)00495-X [pii]
AID - 10.1016/j.jmb.2010.05.016 [doi]
PST - ppublish
SO  - J Mol Biol. 2010 Jul 9;400(2):231-43. doi: 10.1016/j.jmb.2010.05.016. Epub 2010 
      May 13.