5IQP

14-3-3 PROTEIN TAU ISOFORM

Summary for 5IQP

• Entry DOI: 10.2210/pdb5iqp/pdb
• Descriptor: 14-3-3 protein theta, SULFATE ION (3 entities in total)
• Functional Keywords: multiple signalling pathways, phosphorylation, binding to kinase, signaling protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P27348
• Total number of polymer chains: 2
• Total formula weight: 55782.59

Authors

Xiao, B.,Smerdon, S.J.,Gamblin, S.J. (deposition date: 2016-03-11, release date: 2016-03-23, Last modification date: 2024-05-08)

Primary citation

Xiao, B.,Smerdon, S.J.,Jones, D.H.,Dodson, G.G.,Soneji, Y.,Aitken, A.,Gamblin, S.J.
Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
Nature, 376:188-191, 1995

PubMed Abstract: A broad range of organisms and tissues contain 14-3-3 proteins, which have been associated with many diverse functions including critical roles in signal transduction pathways, exocytosis and cell cycle regulation. We report here the crystal structure of the human T-cell 14-3-3 isoform (tau) dimer at 2.6 A resolution. Each monomer (Mr 28K) is composed of an unusual arrangement of nine antiparallel alpha-helices organized as two structural domains. The dimer creates a large, negatively charged channel approximately 35 A broad, 35 A wide and 20 A deep. Overall, invariant residues line the interior of this channel whereas the more variable residues are distributed on the outer surface. At the base of this channel is a 16-residue segment of 14-3-3 which has been implicated in the binding of 14-3-3 to protein kinase C.

PubMed: 7603573
DOI: 10.1038/376188a0

Experimental method

X-RAY DIFFRACTION (2.602 Å)