胶原纤维
胶原VI
化学
胶原蛋白,I型,α1
分子生物学
生物
细胞外基质
生物化学
解剖
出处
期刊:Matrix Biology
[Elsevier]
日期:2002-01-01
卷期号:21 (1): 63-66
被引量:41
标识
DOI:10.1016/s0945-053x(01)00176-7
摘要
The FACIT collagens bind to the surface of collagen fibrils linking them with other matrix molecules. Bioinformatics analysis of cDNA clone DKFZp564B052 showed that it resembled the FACIT collagens and was therefore designated collagen α1(XXI). Phylogenetic analyses of the N-terminal NC3 domains of α1(XXI) and other FACIT collagens showed that (i) α1(XXI) clustered with the FACIT collagens; (ii) collagen α1(XXI) arose before the divergence of α1(XII), α1(XIV) and α1(XX); (iii) collagen α1(XIV) derived from the C-terminal region of the NC3 domain of a collagen α1(XII)-like molecule; and (iv) collagen α1(XX) derived from a collagen α1(XIV)-like molecule. This study provides a framework for the evolution of the FACIT collagens which will be of value in linking NC3 domains with their functions.
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