Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen

被引：207

作者：

Scott, JE

机构：

[1] Department of Chemical Morphology, Chemistry Building, Manchester University, Manchester M13 9PL, Oxford Road

来源：

BIOCHEMISTRY | 1996年 / 35卷 / 27期

关键词：

D O I：

10.1021/bi960773t

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The small proteoglycans proteodermatan and proteokeratan sulfates organize collagen fibrils in extracellular matrix [Scott, J. E. (1992) FASEB J. 6, 2639-2645], thus helping to maintain tissue shape. Their interaction with fibrils is probably via the protein. They have been examined by rotary shadowing-electron microscopy, which showed that these leucine-rich-repeat proteins are horseshoe shaped. Morphometry and comparison with polypeptide sequences suggest ways in which decorin could interact with tissue collagen fibrils, It is proposed that decorin is a bidentate ligand attached to two parallel neighboring collagen molecules in the fibril, helping to stabilize fibrils and orient fibrillogenesis.

引用

页码：8795 / 8799

页数：5

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