3MHR

14-3-3 sigma in complex with YAP pS127-peptide

Summary for 3MHR

• Entry DOI: 10.2210/pdb3mhr/pdb
• Related: 2O02 2O98 3CU8 3E6Y 3LW1
• Descriptor: 14-3-3 protein sigma, YAP phosphopeptide, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: 14-3-3, yap, adapter protein, protein-protein interaction, peptide binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P31947
• Total number of polymer chains: 2
• Total formula weight: 28249.43

Authors

Schumacher, B.,Skwarczynska, M.,Rose, R.,Ottmann, C. (deposition date: 2010-04-08, release date: 2010-09-15, Last modification date: 2024-10-30)

Primary citation

Schumacher, B.,Skwarczynska, M.,Rose, R.,Ottmann, C.
Structure of a 14-3-3[sigma]-YAP phosphopeptide complex at 1.15 A resolution
Acta Crystallogr.,Sect.F, 66:978-984, 2010

PubMed Abstract: The 14-3-3 proteins are a class of eukaryotic acidic adapter proteins, with seven isoforms in humans. 14-3-3 proteins mediate their biological function by binding to target proteins and influencing their activity. They are involved in pivotal pathways in the cell such as signal transduction, gene expression, enzyme activation, cell division and apoptosis. The Yes-associated protein (YAP) is a WW-domain protein that exists in two transcript variants of 48 and 54 kDa in humans. By transducing signals from the cytoplasm to the nucleus, YAP is important for transcriptional regulation. In both variants, interaction with 14-3-3 proteins after phosphorylation of Ser127 is important for nucleocytoplasmic trafficking, via which the localization of YAP is controlled. In this study, 14-3-3σ has been cloned, purified and crystallized in complex with a phosphopeptide from the YAP 14-3-3-binding domain, which led to a crystal that diffracted to 1.15 A resolution. The crystals belonged to space group C222(1), with unit-cell parameters a=82.3, b=112.1, c=62.9 A.

PubMed: 20823509
DOI: 10.1107/S1744309110025479

Experimental method

X-RAY DIFFRACTION (1.15 Å)