The PB1 (Phox and Bem1) domain, comprising about 80 amino acid residues, isconserved among animals, fungi, amoebas, and plants. It functions as a proteinbinding module through PB1-mediated heterodimerization or homo-oligomerization[1, 2, 3, 4].

The PB1 domains adopt an ubiquitin-like beta-grasp fold, containing two alphahelices and a mixed five-stranded beta sheet. The beta-sheethas a convex surface, and alpha1 fits into the cavity formed by the sheet. PB1domains may display an acidic surface (type I), a basic surface (tape II), orboth surfaces (type I/II) on opposite faces of the domain structure to allowfor front-to-back orientation of multiple PB1 domains [5, 5, 5, 5, 5].

1. Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants. Sci. STKE 2007, re6
2. Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. J. Biol. Chem. 280, 9653-61
3. Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. EMBO J. 20, 3947-56
4. Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression. Proc. Natl. Acad. Sci. U.S.A. 111, 5427-32
5. Structural basis for oligomerization of auxin transcriptional regulators. Nat Commun 5, 3617

The PB1 (Phox and Bem1) domain, comprising about 80 amino acid residues, isconserved among animal
Show more...

Download genes (select columns to include)