Center for Matrix Biology - Vanderbilt University and Medical Center

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

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.

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