Water-Refined Solution Structure of the Human Grb7-SH2 Domain in Complex with the erbB2 Receptor Peptide pY1139

Authors: C. Pias, Sally; L. Johnson, Dennis; E. Smith, David; A. Lyons, Barbara

Source: Protein and Peptide Letters, Volume 19, Number 8, August 2012 , pp. 832-838(7)

Publisher: Bentham Science Publishers

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Abstract:

We report a refinement in implicit water of the previously published solution structure of the Grb7-SH2 domain bound to the erbB2 receptor peptide pY1139. Structure quality measures indicate substantial improvement, with residues in the most favored regions of the Ramachandran plot increasing by 14 % and with WHAT IF statistics (Vriend, G. J. Mol. Graph., 1990, 8(1), 52-56) falling closer to expected values for well-refined structures.

Keywords: Molecular dynamics simulations; NMR refinement; SH2 domain; water refinement; Grb7 protein; signaling pathways; breast cancer; tumor tissues; ligand-bound Grb7-SH2 domain; focal adhesion kinase (FAK)

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986612801619543

Publication date: 2012-08-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.