title: Collagens.
abstract: The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three alpha 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.
authors.affiliation: Department of Pharmacology and Toxicology, Rutgers University, Piscataway, NJ, USA. magordon@eohsi.rutgers.edu
authors.forename: Marion K
authors.initials: MK
authors.lastname: Gordon
authors.forename: Rita A
authors.initials: RA
authors.lastname: Hahn
mesh_terms: D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D006909:Hydroxyproline / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D013329:Structure-Activity Relationship
chemical_list: D003094:Collagen; D006909:Hydroxyproline
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