Collagen 相關
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As the main component of connective tissue, it is the most abundant protein in mammals, [1] making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril [2] known as a collagen helix.
Collagen IV has been the focus of extensive research ranging from biochemistry perspectives, to pathology, and genetic disorders. This is the only collagen type that is encoded by six different genes. The six α-chains of collagen IV can recognize each other with.
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Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. COL1A1 encodes the major component of type I collagen , the fibrillar collagen found in most connective tissues , including cartilage .
- COL1A1, EDSC, OI1, OI2, OI3, OI4, collagen type I alpha 1, collagen type I alpha 1 chain, EDSARTH1, CAFYD
Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (), each called an alpha 1 chain of type III collagen. Formally, the monomers are called collagen type III, alpha-1 chain and in humans are encoded by the COL3A1 gene.
- COL3A1, EDS4A, collagen type III alpha 1, collagen type III alpha 1 chain, EDSVASC, PMGEDSV
InterPro. Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage. Type II collagen is organised into fibrils.
In molecular biology, the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, including type I collagen. In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data.