Structure of coiled beta-beta-hairpins and beta-beta-corners

FEBS Lett. 1991 Jun 24;284(2):288-92. doi: 10.1016/0014-5793(91)80706-9.

Abstract

Two types of super-secondary structure, coiled beta-beta-hairpins and beta-beta-corners, are considered in this paper. A beta-beta-corner can be represented as a long beta-beta-hairpin folded orthogonally on itself so that the strands, when passing from one layer to the other, rotate in a right-handed direction about an imaginary axis. It is shown that a beta-beta-hairpin, forming a coiled coil structure or a beta-beta-corner, is right-handed when viewed from the concave side. These unique arrangements of beta-strands in the coiled beta-beta-hairpins and beta-beta-corners are of particular value in protein modelling and prediction.

Publication types

  • Review

MeSH terms

  • Alcohol Dehydrogenase / chemistry
  • Endopeptidases / chemistry
  • Interleukin-1 / chemistry
  • L-Lactate Dehydrogenase / chemistry
  • Protein Conformation*
  • Ribonucleases / chemistry
  • Trypsin Inhibitors / chemistry

Substances

  • Interleukin-1
  • Trypsin Inhibitors
  • Alcohol Dehydrogenase
  • L-Lactate Dehydrogenase
  • Ribonucleases
  • Endopeptidases