title: Protein evolution. On the ancestry of barrels.
abstract: Most proteins consist of several domains linked together in a single polypeptide chain, and many of these proteins have evolved by gene duplication and fusion. Miles and Davies discuss the study by Lang et al., who show that this type of protein evolution may also occur in b/a barrel proteins, a common single-domain protein fold. Other single domain proteins may have arisen from similar evolutionary mechanisms.
authors.affiliation: NIH, Bethesda, MD 20892-0830, USA. edithm@intra.niddk.nih.gov
authors.forename: E W
authors.initials: EW
authors.lastname: Miles
authors.forename: D R
authors.initials: DR
authors.lastname: Davies
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020816:Amino Acid Motifs; D000619:Aminohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002384:Catalysis; D018360:Crystallography, X-Ray; D019281:Dimerization; D019143:Evolution, Molecular; D020440:Gene Duplication; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011995:Recombination, Genetic; D020124:Thermotoga maritima / Q000201:enzymology
chemical_list: C087227:imidazole glycerol phosphate synthase; D000619:Aminohydrolases; D019747:Aldose-Ketose Isomerases; C079656:Phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxiamide isomerase