Defective protein folding as a basis of human disease.
The ability of a polypeptide to fold into a unique, functional, three-dimensional structure in vivo is dependent upon its amino acid sequence and the function of molecular chaperone proteins and enzymes that catalyse folding. Intense study of the physical chemistry and cell biology of folding have greatly aided our understanding of the mechanisms normally employed. Evidence is accumulating that many disease-causing mutations and modifications exert their effects by altering protein folding. Here we discuss the pathobiology of these processes.
Thomas
P J
PJ
Department of Physiology, University of Texas Southwestern Medical Center at Dallas 75235-9040, USA.
Qu
B H
BH
Pedersen
P L
PL
D000591:Amino Acid Isomerases / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D003550:Cystic Fibrosis / Q000378:metabolism; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry / Q000378:metabolism; D004194:Disease / Q000209:etiology*; D006801:Humans; D007535:Isomerases / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D017434:Protein Structure, Tertiary
C505032:CFTR protein, human; D002352:Carrier Proteins; D018832:Molecular Chaperones; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D007535:Isomerases; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases