Assignment of disulfide bonds in corticotropin-releasing factor-binding protein.
We have previously isolated, cloned, and characterized a protein that specifically binds and inactivates the peptide corticotropin-releasing factor. The integrity of the disulfide bonds in the binding protein is essential for this activity as reduction abolishes the protein's ability to bind corticotropin-releasing factor. The disulfide arrangement of the 10 cysteines present in the mature protein was established by analysis of proteolytically cleaved protein and sequence analysis of cystine containing fragments. A pattern is observed where each cysteine is connected to the next one in a sequential manner. Inspection of the genomic DNA encoding for this protein reveals that four of the domains defined by disulfide linkage coincide with four different exons.
Fischer
W H
WH
Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, California 92037.
Behan
D P
DP
Park
M
M
Potter
E
E
Lowry
P J
PJ
Vale
W
W
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D011994:Recombinant Proteins; D014162:Transfection
D002352:Carrier Proteins; D004220:Disulfides; D010446:Peptide Fragments; D011994:Recombinant Proteins; C067133:corticotropin releasing factor-binding protein