Jj. Calvete et al., The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom, PROTEIN SCI, 9(7), 2000, pp. 1365-1373
The disulfide bond pattern of catrocollastatin-C was determined by N-termin
al sequencing and mass spectrometry. The N-terminal disintegrin-like domain
is a compact structure including eight disulfide bonds, seven of them in t
he same pattern as the disintegrin bitistatin. The protein has two extra cy
steine residues (XIII and XVI) that form an additional disulfide bond that
is characteristically found in the disintegrin-like domains of cellular met
alloproteinases (ADAMs) and PIII snake venom Zn-metalloproteinases (SVMPs),
The C-terminal cysteine-rich domain of catrocollastatin-C contains five di
sulfide bonds between nearest-neighbor cysteines and a long range disulfide
bridge between CysV and CysX. These results provide structural evidence fo
r a redefinition of the disintegrin-like and cysteine-rich domain boundarie
s. An evolutionary pathway fur ADAMs, PIII, and PII SVMPs based on disulfid
e bond engineering is also proposed.