Implications of SH3 domain structure and dynamics for protein regulation and drug design |
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Authors: | William H. Gmeiner David A. Horita |
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Affiliation: | (1) Department of Biochemistry, Wake Forest University School of Medicine, 27157 Winston-Salem, NC |
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Abstract: | SH3 Domains provide interesting targets for investigations of protein structure and dynamics because of their compact size and importance for signal transduction. The present review summarizes recent research investigating SH3 domain structure and dynamics, the discovery of novel SH3 domains, the role of SH3 domains in disease, and progress in targeting SH3 domains for the development of novel therapeutics. Particular emphasis is placed on the unfolding/refolding characteristics of SH3 domains and the potential importance of these processes for regulation of signal transduction. |
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Keywords: | SH3 domain NMR signal Transduction Drug Design Protein Dynamics |
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