TY - JOUR
T1 - Identification and characterization of modular domains that bind ubiquitin
AU - French, Michael
AU - Swanson, Kurt
AU - Shih, Susan C.
AU - Radhakrishnan, Ishwar
AU - Hicke, Linda
N1 - Funding Information:
This work was supported by grants from the National Institutes of Health to I. R. and L. H. K. A. S. was supported by an NIH Molecular Biophysics training grant. I. R. is a Scholar of the Leukemia and Lymphoma Society. Support from the Robert H. Lurie Comprehensive Cancer Center for structural biology research at Northwestern University is gratefully acknowledged.
PY - 2005
Y1 - 2005
N2 - To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.
AB - To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.
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U2 - 10.1016/S0076-6879(05)99009-5
DO - 10.1016/S0076-6879(05)99009-5
M3 - Review article
C2 - 16338353
AN - SCOPUS:28844453261
VL - 399
SP - 135
EP - 157
JO - Methods in Enzymology
JF - Methods in Enzymology
SN - 0076-6879
M1 - 9
ER -