Collagen type I contributes maximum to the fibrous protein content in mammals.
It is also present in arteries and extracellular matrix.
The protein has an elongated cylindrical structure with tapering ends.
It possess a left-handed helix with three polyproline II-type polypeptide strands.
Type I collagen [1α(I)]2α2 is distributed throughout the body. This fibrillar collagen is found in dermis, bone, tendon, ligament, dentin, fasciae, sclera, cornea, organ capsules and fibrous cartilage. It appears in tissues as the classically designated collagen fibers which are formed from densely-packed thin striated fibrils with marked variation in diameter. Collagen I is synthesized mainly by fibroblasts, osteoblasts, odontoblasts and chondroblasts.Collagen type Iα1 (COL1A1) is encoded by the gene mapped to human chromosome 17q21.33.
It is the most abundant extracellular matrix (ECM) protein in humans.
Type 1 collagen is the major structural protein of bone, tendon, skin and cornea. The encoded protein is a heterotrimer consisting of two α1-chains and one α2-chain.