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首页> 外文期刊>Journal of Cellular Physiology >The histidine triad superfamily of nucleotide-binding proteins.
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The histidine triad superfamily of nucleotide-binding proteins.

机译：组氨酸三合会的总科nucleotide-binding蛋白质。

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摘要

Histidine triad (HIT) proteins were until recently a superfamily of proteins that shared only sequence motifs. Crystal structures of nucleotide-bound forms of histidine triad nucleotide-binding protein (Hint) demonstrated that the conserved residues in HIT proteins are responsible for their distinctive, dimeric, 10-stranded half-barrel structures that form two identical purine nucleotide-binding sites. Hint-related proteins, found in all forms of life, and fragile histidine triad (Fhit)-related proteins, found in animals and fungi, represent the two main branches of the HIT superfamily. Hint homologs are intracellular receptors for purine mononucleotides whose cellular function remains elusive. Fhit homologs bind and cleave diadenosine polyphosphates (Ap(n)A) such as ApppA and AppppA. Fhit-Ap(n)A complexes appear to function in a proapoptotic tumor suppression pathway in epithelial tissues. In invertebrates, Fhit homologs are encoded as fusion proteins with proteins related to plant and bacterial nitrilases that are candidate signaling partners in tumor suppression. Copyright 1999 Wiley-Liss, Inc.
机译：组氨酸三合会(打击)蛋白质是直到最近蛋白质超家族,共享序列图案。nucleotide-bound组氨酸三元组的形式nucleotide-binding蛋白(提示)守恒的残留的蛋白质负责他们的独特的、二聚的10-stranded half-barrel结构两种形式相同的嘌呤nucleotide-binding网站。Hint-related蛋白质,在所有形式的发现生活,脆性组氨酸三(Fhit) -相关蛋白质,发现动物和真菌,代表达到总科的两个主要分支。提示同系物是细胞内的受体嘌呤单核苷酸的细胞功能仍然是难以捉摸的。diadenosine聚磷酸盐(美联社(n))如ApppA和AppppA。proapoptotic肿瘤抑制功能通路在上皮组织。Fhit基因同源染色体编码为融合蛋白蛋白质与植物和细菌有关腈水解酶候选信号的伙伴在肿瘤的抑制。公司。

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