Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation.
10.1007/s13238-012-2917-5
- Author:
Ming FANG
1
;
Reed JACOB
;
Owen MCDOUGAL
;
Julia Thom OXFORD
Author Information
1. Department of Biological Sciences, Boise State University, Boise, ID 83725, USA.
- Publication Type:Journal Article
- MeSH:
Alternative Splicing;
genetics;
Animals;
Fibrillar Collagens;
chemistry;
genetics;
metabolism;
Humans;
Sulfates;
chemistry;
metabolism;
Surface Properties;
Tyrosine;
analogs & derivatives;
chemistry;
metabolism
- From:
Protein & Cell
2012;3(6):419-433
- CountryChina
- Language:English
-
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.
