Coiled coils in both intracellular vesicle and viral membrane fusion

Article Abstract:

The molecular arrangement of protein complexes engaged in neurotransmitter release and intracellular vesicular flow has been found to be similar to the structures of certain virus membrane fusion proteins. This arrangement is hypothesized to result in close membrane apposition since the complexes are organized for membrane fusion. Results of a study show that complexes from synapses and intracellular vesicles and the membrane fusion subunits of a set of virus glycoproteins create rod-formed alpha-helical bundles. Although they are quite dissimilar in structure, these bundles seem to possess the membrane-anchoring sequences at one of the rod ends.

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Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation

Article Abstract:

A study was conducted to characterize and compare the three-dimensional structure of ectodomain of the precursor influenza HA0 viral membrane-fusion glycoprotein with that of cleaved HA. The cleavage site resulted in structural rearrangements in which the nonpolar amino acids near the amino terminus bury ionizable residues in the cavity that were implicated in the low-pH-induced conformation change.

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T cell receptor-MHC interactions up close

Article Abstract:

Crystal structures of alphabeta T cell receptors, bound to MHC I and II molecules along with bound antigenic peptides, demonstrate the atomic contacts, which illustrate MHC restricted T cell recognition sites.

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