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The collagen protein is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). [23] The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene. [5] It is composed of a triple helical, collagenous domain flanked by two non-collagenous domains, and functions as an anchoring fibril between the dermal-epidermal junction in the basement membrane. [ 6 ]
Type III collagen is a known ligand for the receptor GRP56. The first single base mutation in the COL3A1 gene was reported in 1989 in a patient with vEDS and changed a glycine amino acid to a serine [ 20 ] Since then, over 600 different mutations have been characterized in the COL3A1 gene. [ 21 ]
In addition, ovotransferrin is glycosylated by the N-linkage to the amino acid known as asparagine, meaning that the glycan, the carbohydrate chain, is attached to the nitrogen on the amino acid. Asparagine, found abundantly in asparagus (hence, its name), is one of twenty of the most common amino acids and was the first amino acid to be ...
This mutation substitutes the amino acid cysteine for the amino acid arginine at position 134 in the protein made by the gene. (The mutation can also be written as Arg134Cys.) The altered protein interacts abnormally with other collagen-building proteins, disrupting the structure of type I collagen fibrils and trapping collagen in the cell.
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in ...
Type IV collagen is expressed close to the cancer cells in vivo, forming basement membrane like structures on the cancer cell surface that colocalize with the integrin receptors. The interaction between type IV collagen produced by the cancer cell, and integrins on the surface of the cancer cells, are important for continuous cancer cell growth ...
Mutations in the COL11A2 gene have been shown to cause hearing loss without other signs or symptoms (nonsyndromic deafness autosomal dominant) in two large families.One family carries a mutation that substitutes the amino acid cysteine (a building block of proteins) for the amino acid arginine at position 549 (written as Arg549Cys) in the alpha 2 chain of type XI collagen.