Crystal structure of the zeta isoform of the 14-3-3 protein
Article Abstract:
The zeta isoform of the mammalian 14-3-3 protein contains two subunits each of which are composed of nine antiparallel helices forming a palisade around an amphipathic groove. The carboxy-terminal loop sequence of the protein is acidic and interacts with the basic residues present at the top of the groove. The ligand binding surface has been conserved during evolution in both vertebrates and plants. The 14-3-3 proteins bind to the products of the oncogene and proto-oncogene.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Crystal structure of a complex between anthrax toxin and its host cell receptor
Article Abstract:
The crystal structure of the protective antigen (PA)-CMG2 complex at 2.5A resolution, where CMG2 is a host cell receptor is presented. The study of the structure shows the presence of an extensive receptor-pathogen interaction surface, which imitates the nonpathogenic recognition of the extracellular matrix by integrins.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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- Abstracts: Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Switch-based mechanism of kinesin motors
- Abstracts: Crystal structure of the anthrax toxin protective antigen. Crystal structure of the anthrax lethal factor. Identification of the cellular receptor for anthrax toxin