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Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.
TLDR
Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
Structure and function of Toll receptors and their ligands.
TLDR
How microbial structures as different as nucleic acids and lipoproteins can be recognized by the extracellular domains of Toll receptors is discussed and the emerging area of cross talk in the Toll pathways is assessed.
Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling
TLDR
It is shown that, in contrast to the human Toll-like receptors, Drosophila Toll requires only an endogenous protein ligand for activation and signaling.
Assembly and localization of Toll-like receptor signalling complexes
TLDR
The molecular basis for the recognition of pathogen-associated molecular patterns, the nature of the protein complexes that mediate signalling, and the way in which signals are regulated and integrated at the level of allosteric assembly, post-translational modification and subcellular trafficking of the components of the signalling complexes are discussed.
Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila.
TLDR
It is proposed that muscle amphiphysin is not involved in clathrin-mediated endocytosis, but in the structural organization of the membrane-bound compartments of the excitation-contraction coupling machinery of muscles.
The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction.
TLDR
Observations provide clear evidence that the myristoylation of TRAM targets it to the plasma membrane, where it is essential for L PS responses through the TLR4 signal transduction pathway, and suggest a hitherto unappreciated manner in which LPS responses can be regulated.
Structural Complementarity of Toll/Interleukin-1 Receptor Domains in Toll-like Receptors and the Adaptors Mal and MyD88*
The Toll/interleukin 1 receptor (TIR) domain is a region found in the cytoplasmic tails of members of the Toll-like receptor/interleukin-1 receptor superfamily. The domain is essential for signaling
An Oligomeric Signaling Platform Formed by the Toll-like Receptor Signal Transducers MyD88 and IRAK-4*
TLDR
These findings indicate that TLR activation causes the formation of a highly oligomeric signaling platform analogous to the death-inducing signaling complex of the Fas receptor pathway.
The molecular basis of the host response to lipopolysaccharide
TLDR
This Progress article focuses on recent exciting data that have revealed the structural basis of TLR4–MD2 recognition of LPS.
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