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@ARTICLE{KazemeinJasemi:904331,
      author       = {Kazemein Jasemi, Neda S. and Herrmann, Christian and
                      Magdalena Estirado, Eva and Gremer, Lothar and Willbold,
                      Dieter and Brunsveld, Luc and Dvorsky, Radovan and Ahmadian,
                      Mohammad R.},
      title        = {{T}he intramolecular allostery of {GRB}2 governing its
                      interaction with {SOS}1 is modulated by phosphotyrosine
                      ligands},
      journal      = {Biochemical journal},
      volume       = {478},
      number       = {14},
      issn         = {0006-2936},
      address      = {London},
      publisher    = {Portland Press},
      reportid     = {FZJ-2021-05901},
      pages        = {2793 - 2809},
      year         = {2021},
      note         = {Kein Post-print vorhanden},
      abstract     = {Growth factor receptor-bound protein 2 (GRB2) is a
                      trivalent adaptor protein and a key element in signal
                      transduction. It interacts via its flanking nSH3 and cSH3
                      domains with the proline-rich domain (PRD) of the RAS
                      activator SOS1 and via its central SH2 domain with
                      phosphorylated tyrosine residues of receptor tyrosine
                      kinases (RTKs; e.g. HER2). The elucidation of structural
                      organization and mechanistic insights into GRB2
                      interactions, however, remain challenging due to their
                      inherent flexibility. This study represents an important
                      advance in our mechanistic understanding of how GRB2 links
                      RTKs to SOS1. Accordingly, it can be proposed that (1) HER2
                      pYP-bound SH2 potentiates GRB2 SH3 domain interactions with
                      SOS1 (an allosteric mechanism); (2) the SH2 domain blocks
                      cSH3, enabling nSH3 to bind SOS1 first before cSH3 follows
                      (an avidity-based mechanism); and (3) the allosteric
                      behavior of cSH3 to other domains appears to be
                      unidirectional, although there is an allosteric effect
                      between the SH2 and SH3 domains.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34232285},
      UT           = {WOS:000683548100006},
      doi          = {10.1042/BCJ20210105},
      url          = {https://juser.fz-juelich.de/record/904331},
}