The structural and functional organization of intramolecular chaperones: the N-terminal propeptides which mediate protein folding.
A large number of prokaryotic as well as eukaryotic proteins are produced with amino terminal propeptides. These amino-terminal extensions are essential for mediating proper folding of their corresponding proteins and are also termed as intramolecular chaperones. Though these propeptides are highly specific and unique in their function, several common features have been identified and indicate that the overall mechanism by which they function may be very similar.
Shinde
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U
Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854.
Inouye
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M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D018833:Chaperonins; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D010940:Plant Proteins; D011506:Proteins; D018833:Chaperonins