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@ARTICLE{Porter2005454,
author={Porter, C.J. and Wilce, M.C.J. and Mackay, J.P. and Leedman, P. and Wilce, J.A.},
title={Grb7-SH2 domain dimerisation is affected by a single point mutation},
journal={European Biophysics Journal},
year={2005},
volume={34},
number={5},
pages={454-460},
doi={10.1007/s00249-005-0480-1},
note={cited By 24},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-22844435175&doi=10.1007%2fs00249-005-0480-1&partnerID=40&md5=80176ab821b1958b0ba96861c0a7da52},
affiliation={School of Biomedical and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Perth, WA 6009, Australia; School of Medicine and Pharmacology, University of Western Australia, 35 Stirling Highway, Perth, WA 6009, Australia; Western Australian Institute for Medical Research, University of Western Australia, 35 Stirling Highway, Perth, WA 6009, Australia; School of Molecular and Microbial Biosciences, University of Sydney, Sydney, NSW 2006, Australia},
abstract={Growth factor receptor bound protein 7 (Grb7) is an adaptor protein that is co-overexpressed and forms a tight complex with the ErbB2 receptor in a number of breast tumours and breast cancer cell lines. The interaction of Grb7 with the ErbB2 receptor is mediated via its Src homology 2 (SH2) domain. Whilst most SH2 domains exist as monomers, recently reported studies have suggested that the Grb7-SH2 domain exists as a homodimer. The self-association properties of the Grb7-SH2 domain were therefore studied using sedimentation equilibrium ultracentrifugation. Analysis of the data demonstrated that the Grb7-SH2 domain is dimeric with a dissociation constant of approximately 11 μM. We also demonstrate, using size-exclusion chromatography, that mutation of phenylalanine 511 to an arginine produces a monomeric form of the Grb7-SH2 domain. This mutation represents the first step in the engineering of a Grb7-SH2 domain with good solution properties for further biophysical and structural investigation. © EBSA 2005.},
author_keywords={Analytical ultracentrifugation;  Growth factor receptor bound protein 7;  Protein engineering;  Size-exclusion chromatography;  Src homology 2 domain},
keywords={adaptor protein;  arginine;  dimer;  growth factor receptor;  growth factor receptor bound protein 7;  monomer;  phenylalanine;  unclassified drug, article;  breast cancer;  cancer cell culture;  gel permeation chromatography;  protein domain;  protein engineering;  protein expression;  protein interaction;  sedimentation;  Src homology domain;  ultracentrifugation, Arginine;  Biophysics;  Cell Line, Tumor;  Chromatography;  Dimerization;  Dose-Response Relationship, Drug;  Escherichia coli;  Humans;  Hydrogen-Ion Concentration;  Models, Statistical;  Molecular Conformation;  Mutagenesis, Site-Directed;  Mutation;  Phenylalanine;  Plasmids;  Point Mutation;  Protein Binding;  Protein Engineering;  Protein Structure, Tertiary;  src Homology Domains;  Ultracentrifugation},
correspondence_address1={Wilce, J.A.; School of Biomedical and Chemical Sciences, 35 Stirling Highway, Perth, WA 6009, Australia; email: Jackie.wilce@med.monash.edu.au},
issn={01757571},
coden={EBJOE},
pubmed_id={15841400},
language={English},
abbrev_source_title={Eur. Biophys. J.},
document_type={Article},
source={Scopus},
}