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PB1 Domain

No ImageOne 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.

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.
Examples of Proteins: 
PB1 Domain Proteins
Heterodimerization Partners
Par-6 isoforms PKCzeta, PKClampda
Bem1 Cdc24
p67phox p40phox

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