Similarities of Integumentary Mucin B.1 from Xenopus laevis and Prepro-von Willebrand Factor at Their Amino-terminal Regions*

Similarities of Integumentary Mucin B.1 from Xenopus laevis and Prepro-von Willebrand Factor at Their Amino-terminal Regions*
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非洲爪蟾外皮粘蛋白 B.1 和前血管性血友病因子在氨基末端区域的相似性*

DOI:
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发表时间:
1997
影响因子:
4.8
通讯作者:
W. Hoffmann
W. Hoffmann
中科院分区:
生物学2区
文献类型:
--
作者:
W. Joba;W. Hoffmann

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青蛙表皮粘蛋白B.1(FIM-B. 1)含有多种富含半胱氨酸的模块。在过去,已经发现了一个COOH末端的“胱氨酸结”基序,这是类似于冯维勒布兰德因子,这一地区通常被认为是负责二聚化过程。此外,"补体控制蛋白"基序作为FIM-B. 1中的内部富含半胱氨酸的结构域存在。我们在这里的特点是缺少75%的FIM-B. 1前体的NH2末端的分子克隆。与前冯维勒布兰德因子类似,存在与D结构域相当相似的四个元件(即D1-D2-D'-D3)。这些结构域已被描述为血管性血友病因子多聚化所必需的。因此,FIM-B. 1的一般结构类似于人粘蛋白MUC2以及前冯维勒布兰德因子的一般结构;这三种分子至少似乎共享共同的结构元件,从而允许类似的多聚化机制。
Frog integumentary mucin B.1 (FIM-B.1) contains various cysteine-rich modules. In the past, a COOH-terminal “cystine knot” motif has been found that is similar to von Willebrand factor; this region is generally known to be responsible for dimerization processes. Furthermore, a “complement control protein” motif is present as an internal cysteine-rich domain in FIM-B.1. We characterize here the missing 75% toward the NH2 terminus of the FIM-B.1 precursor by molecular cloning. Analogous to prepro-von Willebrand factor, four elements with considerable similarity to D-domains are present (i.e. D1-D2-D′-D3). These domains have been described as essential for the multimerization of von Willebrand factor. Thus, the general structure of FIM-B.1 resembles that of the human mucin MUC2 as well as prepro-von Willebrand factor; these three molecules at least seem to share common structural elements allowing similar multimerization mechanisms.
DOI: 10.1073/pnas.85.23.8998
发表时间: 1988-12-01
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DOI: --
发表时间: 1991
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