X-ray structures of the universal translation initiation factor IF2/elF5B: conformational changes on GDP and GTP binding
Article Abstract:
Research reveals that the universal translation initiation factor IF2/elF5B, involved in the protein synthesis, is a GTPase enzyme that mediates joining of ribosomal subunits and tRNA binding to ribosomes in pro- and eukaryotic systems. Data are discussed in relation to mechanisms of GTPase function.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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X-ray structures of Myc-Max and Mad-Max recognizing DNA: molecular bases of regulation by proto-oncogenic transcription factors
Article Abstract:
Research has been conducted on Myc-Max and Mad-Max heterodimers which are bound to duplex containing E boxes. The study of the cocrystal structures of these chemoselectively ligated heterodimers is presented.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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Mechanistic link between PKR dimerization, autophosphorylation, and elF2alpha substrate recognition
Article Abstract:
Mutations that activate PKR in the absence of its regulatory domains and map the mutations to an identified dimerization surface on the kinase catalytic domain are identified. An ordered mechanism of PKR activation in which catalytic-domain dimerization triggers Thr446 autophosphorylation and specific elF2alpha substrate recognition is proposed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
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