Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure.

Publication Type:

Journal Article

Authors:

Wang, Jing; Dye, Billy T; Rajashankar, Kanagalaghatta R; Kurinov, Igor; Schulman, Brenda A

Source:

Nat Struct Mol Biol, Volume 16, Issue 9, p.987-9 (2009)

Keywords:

Amino Acid Motifs, Amino Acid Sequence, Anaphase-Promoting Complex-Cyclosome, Apc6 Subunit, Anaphase-Promoting Complex-Cyclosome, Cell Cycle Proteins, Circular Dichroism, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases

Abstract:

<p>The multisubunit anaphase promoting complex (APC) is an essential cell-cycle regulator. Although CDC26 is known to have a role in APC assembly, its molecular function has remained unclear. Biophysical, structural and genetic studies presented here reveal that CDC26 stabilizes the structure of APC6, a core TPR protein required for APC integrity. Notably, CDC26-APC6 association involves an intermolecular TPR mimic composed of one helix from each protein.</p>