Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
Article Abstract:
A study of the crystal structure of the 14-3-3 protein isoform (tau) of the human T cell shows that this protein is in the form of a dimer. Each monomer is composed of two structural domains made of nine antiparallel alpha-helices. A negatively charged channel is formed by the dimer whose interior is lined by invariant residues and the exterior by variant residues. The 16-residue segment present at the base of the channel is probably involved in the binding of the protein to protein kinase C. 14-3-3 proteins activate tryosine and tryptophan hydroxylases and are involved in signal transduction.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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The role of turns in the structure of an alpha-helical protein
Article Abstract:
Interhelical turns in an antiparallel four-helix bundle do not seem to play an important role in its folded structure. Previous research has focused on beta turns connecting antiparallel beta strands. This study looked at the turn connecting helices three and four in cytochrome b-562, and while it was of necessity quite narrow, it implies that individual interhelical turns play a very small role in determining protein structure.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Ice-binding structure and mechanism of an antifreeze protein from winter flounder
Article Abstract:
The structure of the alpha-helical antifreeze protein of winter flounder was analyzed using X-ray crystallography at 1.5-Angstrom resolution. The results show four repeated ice-binding motifs with rigid, flat binding surfaces and elaborate carboxy- and amino-terminal caps. An ice-binding model which accounts for the binding specificity of the antifreeze protein along specific axes of the ice planes is presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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