| Collagen triple helix | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 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.
- ^ Berisio R, Vitagliano L, Mazzarella L, Zagari A (February 2002). "Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)". Protein Sci. 11 (2): 262–70. doi:10.1110/ps.32602. PMC 2373432. PMID 11790836.
- ^ Bhattacharjee A, Bansal M (March 2005). "Collagen structure: the Madras triple helix and the current scenario". IUBMB Life. 57 (3): 161–72. doi:10.1080/15216540500090710. PMID 16036578. S2CID 7211864.
- ^ Saad, Mohamed (Oct 1994). Low resolution structure and packing investigations of collagen crystalline domains in tendon using Synchrotron Radiation X-rays, Structure factors determination, evaluation of Isomorphous Replacement methods and other modeling. PhD Thesis, Université Joseph Fourier Grenoble I. pp. 1–221. doi:10.13140/2.1.4776.7844.