Collagen structure: the Madras triple helix and the current scenario

Bhattacharjee, Arnab ; Bansal, Manju (2005) Collagen structure: the Madras triple helix and the current scenario IUBMB Life, 57 (3). pp. 161-172. ISSN 1521-6543

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This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, first proposed by Ramachandran's group from Madras. The structure is unique among the protein secondary structures in that it requires a very specific tripeptide sequence repeat, with glycine being mandatory at every third position and readily accommodates the imino acids proline/hydroxyproline, at the other two positions. The original structure was postulated to be stabilized by two interchain hydrogen bonds, per tripeptide. Subsequent modeling studies suggested that the triple helix is stabilized by one direct inter chain hydrogen bond as well as water mediated hydrogen bonds. The hydroxyproline residues were also implicated to play an important role in stabilizing the collagen fibres. Several high resolution crystal structures of oligopeptides related to collagen have been determined in the last ten years. Stability of synthetic mimics of collagen has also been extensively studied. These have confirmed the essential correctness of the coiled-coil triple helical structure of collagen, as well as the role of water and hydroxyproline residues, but also indicated additional sequence-dependent features. This review discusses some of these recent results and their implications for collagen fiber formation.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Collagen Structure; Triple Helix; Hydroxyproline; Amino Acid Propensity
ID Code:47428
Deposited On:11 Jul 2011 05:13
Last Modified:11 Jul 2011 05:13

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