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Article
Minor Fibrillar Collagens, Variable Regions Alternative Splicing, Intrinsic Disorder, and Tyrosine Sulfation
Protein & Cell
  • Ming Fang, Boise State University
  • Reed B. Jacob, Boise State University
  • Owen McDougal, Boise State University
  • Julia Oxford, Boise State University
Document Type
Article
Publication Date
6-1-2012
Disciplines
Abstract
Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagens 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 suggest the potential for shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggests modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.
Copyright Statement

This is an author-produced, peer-reviewed version of this article. The final publication is available at www.springerlink.com. Copyright restrictions may apply. DOI: 10.1007/s13238-012-2917-5

Citation Information
Ming Fang, Reed B. Jacob, Owen McDougal and Julia Oxford. "Minor Fibrillar Collagens, Variable Regions Alternative Splicing, Intrinsic Disorder, and Tyrosine Sulfation" Protein & Cell (2012)
Available at: http://works.bepress.com/julia_oxford/21/