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首页> 外文期刊>Journal of Molecular Biology >The structure of the extracellular domain of the jumping translocation breakpoint protein reveals a variation of the midkine fold
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The structure of the extracellular domain of the jumping translocation breakpoint protein reveals a variation of the midkine fold

机译：跳跃易位断点蛋白的胞外域结构揭示了中因子折叠的变异

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摘要

Jumping Translocation Breakpoint (JTB) is an orphan receptor that is conserved from nematodes to humans and whose gene expression in humans is strikingly upregulated in diverse types of cancers. Translocations occur frequently at the hJTB genomic locus, leading to multiple copies of a truncated JTB gene, which potentially encodes a soluble secreted ectodomain. In addition, JTB and its orthologs likely represent a unique and ancient protein family since homologs could not be identified by direct sequence comparison. In the present study, we have determined the NMR solution structure of the N-terminal ectodomain of human JTB, showing that its fold architecture is a new variant of a three-β-strand antiparallel β-meander. The JTB structure has a distant relationship to the midkine/pleiotrophin fold, particularly in the conservation of distinctive disulfide bridge patterns. The structure of this newly characterized small cysteine-rich domain suggests potential involvement of JTB in interactions with proteins or extracellular matrix and may help to uncover the elusive biological functions of this protein.
机译：跳跃易位转折点（Jumping Translocation Breakpoint，JTB）是一种从线虫到人类保守的孤儿受体，其人类基因表达在多种类型的癌症中均显着上调。易位经常发生在hJTB基因组位点，导致截短的JTB基因的多个拷贝，该基因可能编码可溶性分泌的胞外域。此外，JTB及其直系同源物可能代表着独特而古老的蛋白质家族，因为同源物无法通过直接序列比较来鉴定。在本研究中，我们已经确定了人类JTB N端胞外域的NMR溶液结构，表明其折叠结构是三链反平行β链的新变体。 JTB结构与中期因子/促营养素的折叠有遥远的关系，特别是在保留独特的二硫键结构方面。这个新近表征的富含半胱氨酸的小结构域的结构表明，JTB可能参与与蛋白质或细胞外基质的相互作用，并可能有助于揭示该蛋白质难以捉摸的生物学功能。

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