Link protein cDNA sequence reveals a tandemly repeated protein structure.
Link protein cDNA sequence reveals a tandemly repeated protein structure.
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连接蛋白 cDNA 序列揭示了串联重复的蛋白质结构。
DOI：
10.1073/pnas.83.11.3761
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发表时间：
1986
影响因子：
11.1
通讯作者：
Yamada,Y
中科院分区：
文献类型：
--
作者：
Doege,K;Hassell,JR;Caterson,B;Yamada,Y
连接蛋白通过与两种组分结合来稳定软骨蛋白聚糖/透明质酸聚集体。我们用单克隆抗体和多克隆抗血清筛选了从大鼠软骨肉瘤mRNA中制备的λ gt 11表达载体的cDNA文库。我们获得了三分之二的连接蛋白cDNA的克隆，并根据其推导的氨基酸序列对其进行了鉴定。连接蛋白有四种RNA转录物，大小从1.5到5.5个碱基不等。推导的连接蛋白的氨基酸序列显示两个结构域，每个结构域100个残基，共享44%的同源性;在每个结构域内是一个19个残基的伸展74%同源性与其对应物。这种结构表明连接蛋白可能是由基因复制形成的。
Link protein stabilizes the cartilage proteoglycan/hyaluronic acid aggregate by binding to both components. We screened a cDNA library prepared from rat chondrosarcoma mRNA in the lambda gt11 expression vector with monoclonal antibodies and polyclonal antisera to link protein. We obtained a clone for two-thirds of the link protein cDNA and identified it based on its deduced amino acid sequence. There are four RNA transcripts for link protein, ranging from 1.5 to 5.5 kilobases in size. The deduced amino acid sequence for link protein shows two domains of 100 residues each, which share 44% homology; within each domain is a 19-residue stretch 74% homologous with its counterpart. This structure indicates that link protein may have been formed by gene duplication.