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

Jamshid Khoshnoodi, Jean Philippe Cartailler, Keith Alvares, Arthur Veis, Billy G. Hudson*

*Corresponding author for this work

Research output: Contribution to journalShort survey

131 Scopus citations


The α-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 α-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.

Original languageEnglish (US)
Pages (from-to)38117-38121
Number of pages5
JournalJournal of Biological Chemistry
Issue number50
StatePublished - Dec 15 2006


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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