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编码小鼠胶原蛋白VI的α1、α2和α3链的cDNA的克隆与序列分析。

Cloning and sequence analysis of cDNAs encoding the alpha 1, alpha 2 and alpha 3 chains of mouse collagen VI.

作者信息

Zhang R Z, Pan T C, Timpl R, Chu M L

机构信息

Department of Biochemistry and Molecular Biology, Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, PA 19107.

出版信息

Biochem J. 1993 May 1;291 ( Pt 3)(Pt 3):787-92. doi: 10.1042/bj2910787.

Abstract

cDNA clones encoding the alpha 1, alpha 2 and alpha 3 chains of mouse collagen VI have been isolated by screening cDNA libraries with the corresponding human probes. The composite cDNAs for the alpha 1, alpha 2, and alpha 3 chains are 2.5, 1.6 and 2.9 kb in size respectively. The alpha 1 and alpha 2 cDNAs encode the C-terminal portions of the chains as well as the entire 3'-untranslated regions, while the alpha 3 cDNAs encode a central segment of 959 amino acids flanking the triple-helical domain. The deduced amino acid sequences share 86-88% identity with the human counterparts and 67-73% identity with the chicken equivalents. Alignment of the deduced amino acid sequences of mouse, human and chicken collagens reveal that the key features of the protein, including the cysteine residues, imperfections in the Gly-Xaa-Xaa regions, Arg-Gly-Asp sequences and potential N-glycosylation sites, are mostly conserved.

摘要

通过用相应的人类探针筛选cDNA文库,已分离出编码小鼠胶原蛋白VI的α1、α2和α3链的cDNA克隆。α1、α2和α3链的复合cDNA大小分别为2.5、1.6和2.9 kb。α1和α2 cDNA编码链的C末端部分以及整个3'非翻译区,而α3 cDNA编码三联螺旋结构域两侧的959个氨基酸的中央片段。推导的氨基酸序列与人类对应序列具有86-88%的同一性,与鸡的对应序列具有67-73%的同一性。小鼠、人类和鸡胶原蛋白推导的氨基酸序列比对显示,该蛋白质的关键特征,包括半胱氨酸残基、Gly-Xaa-Xaa区域的缺陷、Arg-Gly-Asp序列和潜在的N-糖基化位点,大多是保守的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54db/1132437/33c9528bdf5d/biochemj00112-0131-a.jpg

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