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The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.
- Source :
-
EMBO Journal . 10/1/2003, Vol. 22 Issue 19, p4888-4897. 10p. - Publication Year :
- 2003
-
Abstract
- The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact ββα-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEIN binding
*UBIQUITIN
*GENETIC mutation
*PROTEINS
*BIOCHEMISTRY
*GENETICS
Subjects
Details
- Language :
- English
- ISSN :
- 02614189
- Volume :
- 22
- Issue :
- 19
- Database :
- Academic Search Index
- Journal :
- EMBO Journal
- Publication Type :
- Academic Journal
- Accession number :
- 12956565
- Full Text :
- https://doi.org/10.1093/emboj/cdg475