NDLI: Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide

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Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide

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Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Donaldson, Logan W. Pawson, Tony Gish, Gerald Kay, Lewis E. Forman-kay, Julie D.
Description	Author Affiliation: Donaldson LW ( Department of Molecular and Medical Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8.);
Abstract	On phosphorylation of Y221 by Abelson (Abl) kinase, the Crk-II adapter protein undergoes an intramolecular reorganization initiated by the binding of its own Src homology 2 (SH2) domain to the pY221 site. Conformational changes induced by phosphotyrosine recognition promote the binding of the Src homology 3 (SH3) domain of the Abl tyrosine kinase to a proline-rich loop located between the betaD and betaE strands of the SH2 domain (DE loop). We have determined the NMR solution structure of the ternary complex of the Abl SH3 domain with the Crk SH2 domain bound to a Crk pY221 phosphopeptide. The SH2 domain bridges two ligands that bind at distinct sites. The interaction between the Abl SH3 domain and the Crk SH2 domain is localized to a canonical eight-residue site within the DE loop. From (15)N relaxation experiments, the DE loop of the SH2 domain in the complex displays a significant degree of conformational freedom. The structural and dynamic data therefore indicate that these SH2 and SH3 domains do not assume a unique orientation with respect to one another; rather, they appear to be only tethered via the DE loop. Thus, SH2 domain-SH3 domain interactions do not require additional tertiary contacts or restriction of domain orientation when a recognition motif is presented in a mobile loop. This complex between the Abl SH3 domain, Crk SH2 domain, and Crk phosphopeptide is an example of the extremely modular nature of regulatory proteins that provides a rich repertoire of mechanisms for control of biological function.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Phosphopeptides Chemistry Protein-Tyrosine Kinases Proto-Oncogene Proteins C-abl Proto-Oncogene Proteins Src Homology Domains Amino Acid Sequence Ligands Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Genetics Protein Structure, Tertiary Proto-Oncogene Proteins C-crk Recombinant Fusion Proteins Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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