Vendrell J, Persson B, Avilés F X, Jörnvall H
Departamento de Bioquímica, Universitat Autónoma de Barcelona, Bellaterra, Spain.
Protein Seq Data Anal. 1989 Dec;2(6):461-2.
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.
将羧肽酶原A的94个氨基酸残基的激活片段与其他蛋白质的片段进行了比较。未观察到与其他激活片段有明显的同源性，但补体因子B丝氨酸蛋白酶部分之前的结构域间片段与羧肽酶原A激活片段的N端区域显示出一些结构关系。这可能反映了共同的功能和组织模式。相比之下，目前的比较并未为先前提出的与螺旋-环-螺旋（EF手型）钙结合蛋白的结构同源性提供功能或进一步的序列支持。
