Recent Progress on Collagen Triple Helix Structure, Stability and Assembly

Authors: Rita Berisio; Luigi Vitagliano; Lelio Mazzarella; Adriana Zagari

Source: Protein and Peptide Letters, Volume 9, Number 2, April 2002 , pp. 107-116(10)

Publisher: Bentham Science Publishers

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Abstract:

Collagen is the major structural protein in skin, bone, tendon, cartilage and blood vessels. Its triple helical structure has been long studied by fibre diffraction. More recently, single crystal X-ray diffraction on collagen-like polypeptide models has allowed a significantly improved description of the triple helix and it has shed light on the relationships between triple helix features and stability. This review outlines the current knowledge regarding collagen triple helix structure, stability, and assembly, with a particular emphasis on the latest structural results.

Keywords: collagen triple helix; structural protein; triple helix; fibre diffraction; collagen assembly

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408922

Affiliations: 1: Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 6, I-80134 Napoli.

Publication date: 2002-04-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.