title: New structures of allosteric proteins revealing remarkable conformational changes.
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.
authors.affiliation: Department of Genetics & Microbiology, University of Pavia, Italy. mattevi@ipvgen.unipv.it
authors.forename: A
authors.initials: A
authors.lastname: Mattevi
authors.forename: M
authors.initials: M
authors.lastname: Rizzi
authors.forename: M
authors.initials: M
authors.lastname: Bolognesi
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D000495:Allosteric Site; D018834:Chaperonin 60 / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D011950:Receptors, Cholinergic / Q000737:chemistry
chemical_list: D018834:Chaperonin 60; D011506:Proteins; D011950:Receptors, Cholinergic