Jamshid Khoshnoodi1, Jean-Philippe Cartailler2, Keith Alvares3, Arthur Veis3, and Billy G. Hudson1
1Dept. of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232-2372
2Symmation LLC, PO Box 485, Spring Hill, TN 37174
3Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611
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.