原羧肽酶:与其他蛋白质结构相比的一个激活片段。

Protein sequences & data analysis Pub Date : 1989-12-01
J Vendrell, B Persson, F X Avilés, H Jörnvall
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引用次数: 0

摘要

将原羧肽酶A的94个残基激活片段与其他蛋白的片段进行了比较。补体因子B的丝氨酸蛋白酶部分之前的结构域间片段与原羧肽酶A激活段的n端区域存在一定的结构关系。这可能反映了常见的功能和组织模式。相比之下,目前的比较并没有为先前提出的与螺旋-环-螺旋(EF-hand)钙结合蛋白的结构同源性提供功能或进一步的序列支持。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.

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