title: Procarboxypeptidase A activation segment compared to structures of other proteins.
abstract: 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.
authors.affiliation: Departamento de Bioquímica, Universitat Autónoma de Barcelona, Bellaterra, Spain.
authors.forename: J
authors.initials: J
authors.lastname: Vendrell
authors.forename: B
authors.initials: B
authors.lastname: Persson
authors.forename: F X
authors.initials: FX
authors.lastname: Avilés
authors.forename: H
authors.initials: H
authors.lastname: Jörnvall
mesh_terms: 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
chemical_list: D004792:Enzyme Precursors; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D011415:Complement Factor B