4DAU

Structure of 14-3-3 sigma in complex with PADI6 14-3-3 binding motif I

Summary for 4DAU

• Entry DOI: 10.2210/pdb4dau/pdb
• Related: 1YZ5 4DAT
• Descriptor: 14-3-3 protein sigma, Peptidylarginine Deiminase type VI (3 entities in total)
• Functional Keywords: 14-3-3 fold, protein-protein interaction, signaling protein-protein binding complex, signaling protein/protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P31947
• Total number of polymer chains: 2
• Total formula weight: 27924.41

Authors

Rose, R.,Rose, M.,Ottmann, C. (deposition date: 2012-01-13, release date: 2012-06-13, Last modification date: 2024-10-09)

Primary citation

Rose, R.,Rose, M.,Ottmann, C.
Identification and structural characterization of two 14-3-3 binding sites in the human peptidylarginine deiminase type VI.
J.Struct.Biol., 180:65-72, 2012

PubMed Abstract: The regulation and function of peptidylarginine deiminase isoform VI (PAD6), which is a highly abundant protein associated with the cytoplasmic lattices in mammalian oocytes, is poorly understood so far. It has been shown previously, that 14-3-3 proteins, a class of regulatory adapter proteins ubiquitous in eukaryotes, bind to PAD6 in vivo in a phosphorylation dependent manner. Here we identify possible 14-3-3 binding sites in human PAD6 by in silico methods, looking for conserved, surface exposed serine residues. Two of these sites were confirmed as 14-3-3 binding sites by fluorescence polarization competition and X-ray crystallography. We furthermore suggest a role of RSK-type kinases in the phosphorylation of one of these two binding sites and provide evidence in the form of in vitro kinase assays with p70S6 kinase and RSK1.

PubMed: 22634725
DOI: 10.1016/j.jsb.2012.05.010

Experimental method

X-RAY DIFFRACTION (2 Å)