 PB1 Domain | |
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Structure:
 One NMR structure of the PB1 domain of Bem1p has been solved. The PB1 domain consists of two alpha helices and a mixed, four-stranded, beta-sheet. The domain adopts a beta-grasp fold, similar to those found in ubiquitin and the Ras-binding domain of Raf. However, PB1 domains do not bind Ras related proteins, suggesting the PB1 domain is functionally distinct.
Structure reference:
Terasawa, H. et al. (2002) EMBO. 20(15): 3947-3956. PDB: 1IPG.
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Domain binding and function:
Phox and Bem1 (PB1) domains contain approximately 80 amino acids and are found in a number of cytoplasmic signaling proteins. The PB1 domain is involved in the heterodimerization with a paired PB1 domain, although not all PB1 domains will associate with one another. A highly conserved internal sequence known as OPR, PC or AID motifs is necessary for PB1 domain function. Regions outside the OPR, PC and AID help confer specificity for binding.
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Examples of Proteins:
| PB1 Domain Proteins |
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Heterodimerization Partners |
| Par-6 isoforms |  |
PKCzeta, PKClampda |
| Bem1 | |
Cdc24 |
| p67phox | |
p40phox |
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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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