Collagen helix
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. 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.
| Collagen triple helix | |||||||||||
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Model of a collagen helix. | |||||||||||
| Identifiers | |||||||||||
| Symbol | Collagen | ||||||||||
| Pfam | PF01391 | ||||||||||
| InterPro | IPR008160 | ||||||||||
| SCOP2 | 1a9a / SCOPe / SUPFAM | ||||||||||
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