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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.
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.
The collagen triple helix is a triple helix formed from three separate protein helices, spiraling around the same axis. In the fields of geometry and biochemistry, a triple helix (pl.: triple helices) is a set of three congruent geometrical helices with the same axis, differing by a translation along the axis. This means that each of the ...
Other post-translational modifications occur after the triple helix is formed. The large globular domains from both ends of the molecule are removed by C- and amino(N)-terminal-proteinases to generate triple-helical type III collagen monomers called tropocollagen. In addition, crosslinks form between certain lysine and hydroxylysine residues.
Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits; this gene encodes the alpha 3 subunit. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2
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]
The collagen superfamily consists of 28 different types of collagen. [7] Although the function and hierarchical structure of these collagens may vary, they all share the defining structural feature known as the triple helix, [1] where three left handed polyproline II-type (PPII) helices assemble to form a right-handed supercoiled helical motif.
FACIT collagen (Fibril Associated Collagens with Interrupted Triple helices [1]) is a type of collagen and also a proteoglycan [2] that have two or more triple-helical domains that connect to collagen fibrils and share protein domains with non-collagen matrix molecules. [3]