Collagens
MK Gordon, RA Hahn - Cell and tissue research, 2010 - Springer
MK Gordon, RA Hahn
Cell and tissue research, 2010•SpringerThe collagens represent a family of trimeric extracellular matrix molecules used by cells for
structural integrity and other functions. The three α chains that form the triple helical part of
the molecule are composed of repeating peptide triplets of glycine-XY. X and Y can be any
amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical
regions (ie, Col domains) are non-glycine-XY regions, termed non-collagenous domains.
These frequently contain recognizable peptide modules found in other matrix molecules …
structural integrity and other functions. The three α chains that form the triple helical part of
the molecule are composed of repeating peptide triplets of glycine-XY. X and Y can be any
amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical
regions (ie, Col domains) are non-glycine-XY regions, termed non-collagenous domains.
These frequently contain recognizable peptide modules found in other matrix molecules …
Abstract
The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three α chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are non-glycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.
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