1WMH

Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha

Summary for 1WMH

• Entry DOI: 10.2210/pdb1wmh/pdb
• Related: 1IPG 1OEY 1Q1O 1VD2
• Descriptor: Protein kinase C, iota type, Partitioning defective-6 homolog alpha (3 entities in total)
• Functional Keywords: kinase, pb1 domain, opca motif, apkc, par6, cell polarity, transferase-cell cycle complex, transferase/cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P41743 Q9NPB6
• Total number of polymer chains: 2
• Total formula weight: 19880.63

Authors

Hirano, Y.,Yoshinaga, S.,Suzuki, N.N.,Horiuchi, M.,Kohjima, M.,Takeya, R.,Sumimoto, H.,Inagaki, F. (deposition date: 2004-07-09, release date: 2004-12-07, Last modification date: 2024-03-13)

Primary citation

Hirano, Y.,Yoshinaga, S.,Takeya, R.,Suzuki, N.N.,Horiuchi, M.,Kohjima, M.,Sumimoto, H.,Inagaki, F.
Structure of a Cell Polarity Regulator, a Complex between Atypical PKC and Par6 PB1 Domains
J.Biol.Chem., 280:9653-9661, 2005

PubMed Abstract: A complex of atypical PKC and Par6 is a common regulator for cell polarity-related processes, which is an essential clue to evolutionary conserved cell polarity regulation. Here, we determined the crystal structure of the complex of PKCiota and Par6alpha PB1 domains to a resolution of 1.5 A. Both PB1 domains adopt a ubiquitin fold. PKCiota PB1 presents an OPR, PC, and AID (OPCA) motif, 28 amino acid residues with acidic and hydrophobic residues, which interacts with the conserved lysine residue of Par6alpha PB1 in a front and back manner. On the interface, several salt bridges are formed including the conserved acidic residues on the OPCA motif of PKCiota PB1 and the conserved lysine residue on the Par6alpha PB1. Structural comparison of the PKCiota and Par6alpha PB1 complex with the p40phox and p67phox PB1 domain complex, subunits of neutrophil NADPH oxidase, reveals that the specific interaction is achieved by tilting the interface so that the insertion or extension in the sequence is engaged in the specificity determinant. The PB1 domain develops the interaction surface on the ubiquitin fold to increase the versatility of molecular interaction.

PubMed: 15590654
DOI: 10.1074/jbc.M409823200

Experimental method

X-RAY DIFFRACTION (1.5 Å)