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Open AccessPublisher Correction: Cryo-EM structure of a RAS/RAF recruitment complex
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Open AccessCryo-EM structure of a RAS/RAF recruitment complex
RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, whereupon they initiate signaling through the MAP kinase cascade. Prior structural studies of KRAS with RAF have focused...
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Article
Architecture of autoinhibited and active BRAF–MEK1–14-3-3 complexes
RAF family kinases are RAS-activated switches that initiate signalling through the MAP kinase cascade to control cellular proliferation, differentiation and survival1–3. RAF activity is tightly regulated and inap...
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Open AccessACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils
The coiled-coil (CC) domain is a very important structural unit of proteins that plays critical roles in various biological functions. The major oligomeric state of CCs is a dimer, which can be either parallel...
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Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the ...
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Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8
The mechanism by which the noncanonical E1-like enzyme Atg7 activates ubiquitin-like Atg8 to trigger autophagy has not been well understood. The crystal structures of the N-terminal domain of Atg7 alone and C-...