title: Circular permutations of natural protein sequences: structural evidence.
abstract: Over the past few years, evidence has accumulated that shows that circularly permuted proteins resulting from permutations in their coding genes can indeed occur naturally. In most instances, these circularly permuted amino acid sequences have been detected by sequence alignment of homologous proteins. Circular permutations may escape detection, however, when based on sequence comparisons alone, as recently illustrated by transaldolase, a member of the class I aldolase family.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden. ylva@alfa.mbb.ki.se
authors.forename: Y
authors.initials: Y
authors.lastname: Lindqvist
authors.forename: G
authors.initials: G
authors.lastname: Schneider
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D005964:Glucosyltransferases / Q000737:chemistry / Q000235:genetics; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010456:Peptides, Cyclic / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D014153:Transaldolase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001617:beta-Glucosidase / Q000737:chemistry / Q000145:classification / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D037102:Lectins; D010456:Peptides, Cyclic; D011506:Proteins; D014153:Transaldolase; D005964:Glucosyltransferases; D001617:beta-Glucosidase