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A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp, where X may be any of various other amino acid residues. [24] Proline or hydroxyproline constitute about 1/6 of the total sequence.
Hydroxylysine (Hyl) is an amino acid with the molecular formula C 6 H 14 N 2 O 3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form. [1] It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen. [2] It is biosynthesized from lysine via oxidation by lysyl ...
Chemical Structure of Type I Collagen. Type I collagen has a triple-helical form which is caused by its amino acid composition. Its specific domain follows an order of G-X-Y In which the X and Y slots are occupied by any amino acid other than glycine however these slots are typically occupied by both hydroxyproline and proline, not in any particular order. [5]
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.
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
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