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Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2.

Ivancic M, Daly RJ, Lyons BA
J Biomol NMR 27 205-19 (2003)
Cited: 23 times
EuropePMC logo PMID: 12975581

Abstract

The solution structure of the hGrb7-SH2 domain in complex with a ten amino acid phosphorylated peptide ligand representative of the erbB2 receptor tyrosine kinase (pY1139) is presented as determined by nuclear magnetic resonance methods. The hGrb7-SH2 domain structure reveals the Src homology 2 domain topology consisting of a central beta-sheet capped at each end by an alpha-helix. The presence of a four residue insertion in the region between beta-strand E and the EF loop and resulting influences on the SH2 domain/peptide complex structure are discussed. The binding conformation of the erbB2 peptide is in a beta-turn similar to that found in phosphorylated tyrosine peptides bound to the Grb2-SH2 domain. To our knowledge this is only the second example of an SH2 domain binding its naturally occurring ligands in a turn, instead of extended, conformation. Close contacts between residues responsible for binding specificity in hGrb7-SH2 and the erbB2 peptide are characterized and the potential effect of mutation of these residues on the hGrb7-SH2 domain structure is discussed.

Articles - 1mw4 mentioned but not cited (7)

  1. Loops govern SH2 domain specificity by controlling access to binding pockets. Kaneko T, Huang H, Zhao B, Li L, Liu H, Voss CK, Wu C, Schiller MR, Li SS. Sci Signal 3 ra34 (2010)
  2. Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation. Porter CJ, Matthews JM, Mackay JP, Pursglove SE, Schmidberger JW, Leedman PJ, Pero SC, Krag DN, Wilce MC, Wilce JA. BMC Struct. Biol. 7 58 (2007)
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  4. Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function. Merritt HI, Sawyer N, Arora PS. Pept Sci (Hoboken) 112 e24145 (2020)
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  7. Water-refined solution structure of the human Grb7-SH2 domain in complex with the erbB2 receptor peptide pY1139. Pias SC, Johnson DL, Smith DE, Lyons BA. Protein Pept. Lett. 19 832-838 (2012)


Reviews citing this publication (4)

  1. Grb10 and Grb14: enigmatic regulators of insulin action--and more? Holt LJ, Siddle K. Biochem. J. 388 393-406 (2005)
  2. Progress towards the development of SH2 domain inhibitors. Kraskouskaya D, Duodu E, Arpin CC, Gunning PT. Chem Soc Rev 42 3337-3370 (2013)
  3. Adapter protein connections: the MRL and Grb7 protein families. Holt LJ, Daly RJ. Growth Factors 23 193-201 (2005)
  4. The intertwining of structure and function: proposed helix-swapping of the SH2 domain of Grb7, a regulatory protein implicated in cancer progression and inflammation. Pias S, Peterson TA, Johnson DL, Lyons BA. Crit. Rev. Immunol. 30 299-304 (2010)

Articles citing this publication (12)

  1. SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? Moncoq K, Broutin I, Craescu CT, Vachette P, Ducruix A, Durand D. Biophys. J. 87 4056-4064 (2004)
  2. Grb7-SH2 domain dimerisation is affected by a single point mutation. Porter CJ, Wilce MC, Mackay JP, Leedman P, Wilce JA. Eur. Biophys. J. 34 454-460 (2005)
  3. Structural basis for the binding of high affinity phosphopeptides to Stat3. McMurray JS. Biopolymers 90 69-79 (2008)
  4. Structural basis of binding by cyclic nonphosphorylated peptide antagonists of Grb7 implicated in breast cancer progression. Ambaye ND, Pero SC, Gunzburg MJ, Yap M, Clayton DJ, Del Borgo MP, Perlmutter P, Aguilar MI, Shukla GS, Peletskaya E, Cookson MM, Krag DN, Wilce MC, Wilce JA. J. Mol. Biol. 412 397-411 (2011)
  5. Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex. Ivancic M, Spuches AM, Guth EC, Daugherty MA, Wilcox DE, Lyons BA. Protein Sci. 14 1556-1569 (2005)
  6. Calorimetric investigation of phosphorylated and non-phosphorylated peptide ligand binding to the human Grb7-SH2 domain. Spuches AM, Argiros HJ, Lee KH, Haas LL, Pero SC, Krag DN, Roller PP, Wilcox DE, Lyons BA. J. Mol. Recognit. 20 245-252 (2007)
  7. Calmodulin regulates the translocation of Grb7 into the nucleus. García-Palmero I, Villalobo A. FEBS Lett. 586 1533-1539 (2012)
  8. Interaction of the non-phosphorylated peptide G7-18NATE with Grb7-SH2 domain requires phosphate for enhanced affinity and specificity. Gunzburg MJ, Ambaye ND, Del Borgo MP, Pero SC, Krag DN, Wilce MC, Wilce JA. J. Mol. Recognit. 25 57-67 (2012)
  9. Novel nonphosphorylated peptides with conserved sequences selectively bind to Grb7 SH2 domain with affinity comparable to its phosphorylated ligand. Zhang D, Shao C, Hu S, Ma S, Gao Y. PLoS ONE 7 e29902 (2012)
  10. Binding and function of phosphotyrosines of the Ephrin A2 (EphA2) receptor using synthetic sterile α motif (SAM) domains. Borthakur S, Lee H, Kim S, Wang BC, Buck M. J. Biol. Chem. 289 19694-19703 (2014)
  11. Solution structure of the human Grb14-SH2 domain and comparison with the structures of the human Grb7-SH2/erbB2 peptide complex and human Grb10-SH2 domain. Scharf PJ, Witney J, Daly R, Lyons BA. Protein Sci. 13 2541-2546 (2004)
  12. Grb7 protein RA domain oligomerization. Godamudunage MP, Foster A, Warren D, Lyons BA. J. Mol. Recognit. 30 (2017)


Related citations provided by authors (1)

  1. Assignment of backbone 1H, 13C, and 15N resonances of human Grb7-SH2 domain in complex with a phosphorylated peptide ligand.. Brescia PJ, Ivancic M, Lyons BA J Biomol NMR 23 77-8 (2002)

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