Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8648279 | Journal of Structural Biology | 2017 | 4 Pages |
Abstract
Virus structures were among the earliest illustrations of how regulated protein assembly can proceed by folding of polypeptide-chain segments into complementary sites on partner proteins. I draw on Caspar's image of protein “tentacles” and his metaphor of SV40 pentamers as five-legged, aquatic organisms (“pentopuses”) to suggest a helpful vocabulary. “Tentacular interactions” among component subunits organize most subcellular molecular machines. Their selective advantages include facile regulation of both assembly and disassembly by modifying enzymes and by folding chaperones.
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Molecular Biology
Authors
Stephen C. Harrison,