Structural model of the amino propeptide of collagen XI alpha1 chain with similarity to the LNS domains.

ABSTRACT: 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. Seque

SUBMITTER: Fallahi A 

PROVIDER: S-EPMC2253380 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature