New structures of allosteric proteins revealing remarkable conformational changes

Curr Opin Struct Biol. 1996 Dec;6(6):824-9. doi: 10.1016/s0959-440x(96)80013-3.

Abstract

New three-dimensional structures of allosteric proteins reveal they have a flexible architecture that is instrumental to the regulation of protein function. Highlights are the structures of GroEL, pyruvate kinase, D-3-phosphoglycerate dehydrogenase and the acetylcholine receptor. Furthermore, significant progress in understanding the nature of the intermediates involved in an allosteric reaction has been achieved through recent spectroscopic and crystallographic studies on haemoglobin.

Publication types

  • Review

MeSH terms

  • Allosteric Regulation / physiology
  • Allosteric Site
  • Chaperonin 60 / chemistry
  • Models, Molecular
  • Protein Conformation
  • Protein Folding
  • Proteins / chemistry*
  • Receptors, Cholinergic / chemistry

Substances

  • Chaperonin 60
  • Proteins
  • Receptors, Cholinergic