Molecular recognition in the assembly of collagens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers.

Khoshnoodi J, Cartailler JP, Alvares K, Veis A, Hudson BG
J Biol Chem. 2006 281 (50): 38117-21

PMID: 17082192 · DOI:10.1074/jbc.R600025200

The alpha-chains of the collagen superfamily are encoded with information that specifies self-assembly into fibrils, microfibrils, and networks that have diverse functions in the extracellular matrix. A key self-organizing step, common to all collagen types, is trimerization that selects, binds, and registers cognate alpha-chains for assembly of triple helical protomers that subsequently oligomerize into specific suprastructures. In this article, we review recent findings on the mechanism of chain selection and infer that terminal noncollagenous domains function as recognition modules in trimerization and are therefore key determinants of specificity in the assembly of suprastructures. This mechanism is also illustrated with computer-generated animations.

MeSH Terms (3)

Biopolymers Collagen Protein Conformation

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