Procarboxypeptidase A activation segment compared to structures of other proteins.
The 94-residue activation segment of procarboxypeptidase A was compared with segments of other proteins. No significant homologies were observed towards other activation segments, but an inter-domain segment preceding the serine-protease part of complement factor B showed some structural relationships with the N-terminal region of the procarboxypeptidase A activation segment. This may reflect common functional and organizational patterns. In contrast, the present comparisons do not give functional or further sequence support to previously proposed structural homologies with helix-loop-helix (EF-hand) calcium-binding proteins.
Vendrell
J
J
Departamento de Bioquímica, Universitat Autónoma de Barcelona, Bellaterra, Spain.
Persson
B
B
Avilés
F X
FX
Jörnvall
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D011415:Complement Factor B; D004789:Enzyme Activation; D004792:Enzyme Precursors; D006801:Humans; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D004792:Enzyme Precursors; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D011415:Complement Factor B