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Structural model of the amino propeptide of collagen XI 1 chain with similarity to the LNS domains

¹ Department of Biology and Biomolecular Research Center, ² Materials Science Program, ³ Department of Chemistry, Boise State University, Boise, Idaho 83725, USA

(RECEIVED January 17, 2005; FINAL REVISION March 22, 2005; ACCEPTED March 22, 2005)

Fibrillar collagens are the principal structural molecules of connective tissues. The assembly of collagen fibrils is regulated by quantitatively minor fibrillar collagens, types V and XI. A unique amino-terminal propeptide domain of these collagens has been attributed this regulatory role. The structure of the amino terminal propeptide has yet to be determined. Low sequence similarity necessitated a secondary structure-based method to carry out homology modeling based upon the determined structure of LNS family members, named for a common structure in the laminin LG5 domain, the neurexin 1B domain and the sex hormone binding globulin. Distribution of amino acids within the model suggested glycosaminoglycan interaction and calcium binding. These activities were tested experimentally. Sequence analyses of existing genes for collagens indicate that 16 known collagen chains may contain an LNS domain. A similar approach may prove useful for structure/function studies of similar domains in other collagens with similar domains. This will provide mechanistic details of the organization and assembly of the extracellular matrix and the underlying basis of structural integrity in connective tissues. The absolute requirement for collagen XI in skeletal growth is indicated by collagen XI deficiencies such as chondrodystrophies found in the cho/cho mouse and in humans with Stickler syndrome.

Keywords: type XI collagen; amino propeptide; LNS domain; homology modeling; -sandwich; calcium; heparan sulfate

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051363105.

Reprint requests to: Julia Thom Oxford, Department of Biology, Biomolecular Research Center, Boise State University, Boise, Idaho 83725, USA; e-mail: joxford{at}boisestate.edu; fax: 208 426-4267.

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