Collagen triple helix | |||||||||||
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![]() Model of a collagen helix.[1] | |||||||||||
Identifiers | |||||||||||
Symbol | Collagen | ||||||||||
Pfam | PF01391 | ||||||||||
InterPro | IPR008160 | ||||||||||
SCOP2 | 1a9a / SCOPe / SUPFAM | ||||||||||
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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. 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. Collagen triple helices are often bundled into fibrils which themselves form larger fibres, as in tendons.