 MBT repeat Domain | |
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| Class:Other: Methyl-lysine binding | |
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Structure:
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Domain binding and function:
Malignant brain tumor (MBT)
repeats have been implicated as methyl-lysine binding modules that bind to methylated peptides from the amino-terminal tails of histones H3 and H4. MBT repeats are ~100 amino acid residues in length and are found in the proteome of most metazoans. Each repeat consists of a globular core and an extended arm. Interdigitation between the arms of the three MBT repeats of the polycomb group protein h-l(3)mbt results in a three-leaved propeller with a hollow central cavity. Each repeat harbors a hydrophobic ligand-binding pocket.
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Examples of Proteins:
| MBT proteins |
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Binding Partner |
| CGI-72 |  |
monomethylated histone H3 lysine-4 or H4 lysine-20 |
| L(3)MBTL | |
Histone H3 monomethylated lysine-4 |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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