Protein tentacles

J Struct Biol. 2017 Dec;200(3):244-247. doi: 10.1016/j.jsb.2017.05.012. Epub 2017 May 27.

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.

Keywords: Peptide-surface association; Protein interactions; Regulated assembly; Virus structure.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Molecular Chaperones / chemistry
  • Protein Folding
  • Simian virus 40 / chemistry
  • Viral Proteins / chemistry*
  • Viral Proteins / metabolism
  • Viruses / chemistry*

Substances

  • Molecular Chaperones
  • Viral Proteins