首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Minor fibrillar collagens,variable regions alternative splicing,intrinsic disorder,and tyrosine sulfation
Authors:Ming Fang  Reed Jacob  Owen McDougal  Julia Thom Oxford
Institution:1. Department of Biological Sciences, Boise State University, Boise, ID 83725, USA; 2. Department of Chemistry and Biochemistry, Boise State University, Boise, ID 83725, USA; 3. Biomolecular Research Center, Boise State University, Boise, ID 83725, USA
Abstract:Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.
Keywords:minor fibrillar collagens  variable regions  alternative splicing  fibrillogenesis  heparan sulfate binding sites  intrinsic disorder  tyrosine sulfation  
点击此处可从《蛋白质与细胞》浏览原始摘要信息
点击此处可从《蛋白质与细胞》下载免费的PDF全文
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号