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Visualizing the Induced Binding of SH2-Phosphopeptide
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    Visualizing the Induced Binding of SH2-Phosphopeptide
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    Computational Biochemistry and Biophysics Laboratory (GRIB-IMIM), Universitat Pompeu Fabra, Barcelona Biomedical Research Park, C/Dr. Aiguader 88, 08003 Barcelona, Spain
    Institute of Biomedical Engineering, CNR - National Research Council of Italy, Corso Stati Uniti 4, 35127 Padova, Italy
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    Journal of Chemical Theory and Computation

    Cite this: J. Chem. Theory Comput. 2012, 8, 4, 1171–1175
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    https://doi.org/10.1021/ct300003f
    Published March 10, 2012
    Copyright © 2012 American Chemical Society

    Abstract

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    Approximately 100 proteins in the human genome contain an SH2 domain recognizing small flexible phosphopeptides. It is therefore important to understand in atomistic detail the way these peptides bind and the conformational changes that take place upon binding. Here, we obtained several spontaneous binding events between the p56 lck SH2 domain and the pYEEI peptide within 2 Å RMSD from the crystal structure and with kinetic rates compatible with experiments using high-throughput molecular dynamics simulations. Binding is achieved in two phases, fast contacts of the charged phospho-tyrosine and then rearrangement of the ligand involving the stabilization of two important loops in the SH2 domain. These observations provide insights into the binding pathways and induced conformations of the SH2–phosphopeptide complex which, due to the characteristics of SH2 domains, should be relevant for other SH2 recognition peptides.

    Copyright © 2012 American Chemical Society

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    Supporting Information

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    Data for binding trajectories T1–T5; detailed computational methods; video of the five binding trajectories superimposed; video of the RMSF of domain and ligand during the binding event. The data files containing the binding trajectories are available on request. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 15 publications.

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    Journal of Chemical Theory and Computation

    Cite this: J. Chem. Theory Comput. 2012, 8, 4, 1171–1175
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ct300003f
    Published March 10, 2012
    Copyright © 2012 American Chemical Society

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