The partial amino acid sequence of bovine cartilage proteoglycan, deduced from a cDNA clone, contains numerous Ser-Gly sequences arranged in homologous repeats.

The partial amino acid sequence of bovine cartilage proteoglycan, deduced from a cDNA clone, contains numerous Ser-Gly sequences arranged in homologous repeats.
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从 cDNA 克隆推导出的牛软骨蛋白多糖的部分氨基酸序列包含许多以同源重复排列的 Ser-Gly 序列。

DOI:
10.1042/bj2430255
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发表时间:
1987
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
D. Heinegård
D. Heinegård
中科院分区:
--
文献类型:
--
作者:
A. Oldberg;P. Antonsson;D. Heinegård

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我们已经确定了编码牛软骨聚集蛋白聚糖核心蛋白C-末端区域的部分cDNA克隆的序列。推导的氨基酸序列中含有一个与鸡肝凝集素同源的富含半胱氨酸的区域。这个凝集素同源区域以前已被确定在大鼠和鸡软骨蛋白聚糖。这里提供的牛序列与这个明显的球状区域中的大鼠和鸡氨基酸序列高度同源。含有Ser-Gly序列簇的区域位于凝集素同源结构域的N-末端。这些富含Ser-Gly的片段串联重复排列,约。100个残基长的同源结构域。每个同源结构域由大约一个同源结构域组成。75-残基长的富含Ser-Gly的区域被大约100个氨基酸间隔开。缺少Ser-Gly二肽的25个残基长的片段。这些二肽排列在100个残基长的同源结构域中的10个残基长的片段中。较短的同源片段在每个100个残基长的同源结构域中串联重复约6次。这些重复序列中的丝氨酸残基是硫酸软骨素链的潜在附着位点。
We have determined the sequence of a partial cDNA clone encoding the C-terminal region of bovine cartilage aggregating proteoglycan core protein. The deduced amino acid sequence contains a cysteine-rich region which is homologous with chicken hepatic lectin. This lectin-homologous region has previously been identified in rat and chicken cartilage proteoglycan. The bovine sequence presented here is highly homologous with the rat and chicken amino acid sequences in this apparently globular region. A region containing clusters of Ser-Gly sequences is located N-terminal to the lectin homology domain. These Ser-Gly-rich segments are arranged in tandemly repeated, approx. 100-residue-long, homology domains. Each homology domain consists of an approx. 75-residue-long Ser-Gly-rich region separated by an approx. 25-residue-long segment lacking Ser-Gly dipeptides. These dipeptides are arranged in 10-residue-long segments in the 100-residue-long homology domains. The shorter homologous segments are tandemly repeated some six times in each 100-residue-long homology domain. Serine residues in these repeats are potential attachment sites for chondroitin sulphate chains.