Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.
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McMullen BA, Fujikawa K, Davie EW
Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.
Biochemistry. 1991 Feb 26;30(8):2050-6.
- PubMed ID
- 1998666 [ View in PubMed]
- Abstract
The location of 16 of the 18 disulfide bonds in human plasma prekallikrein was determined by amino acid sequence analysis of cystinyl peptides produced by chemical and enzymatic digestions. A unique structure, named the apple domain, was established for each of the four tandem repeats in the amino-terminal portion of the molecule. The apple domains (90 or 91 amino acids) contain 3 highly conserved disulfide bonds linking the first and sixth, second and fifth, and third and fourth half-cystine residues present in each repeat. The fourth tandem repeat contains an extra disulfide bond that forms a second small loop within the apple domain. The carboxyl-terminal portion of plasma prekallikrein containing the catalytic region of the molecule was found to have disulfide bonds located in positions similar to those of other serine proteases.