PREDICTED STRUCTURE AND BINDING MOTIFS OF COLLAGEN α1(XI).

ABSTRACT: The amino propeptide of collagen α1(XI) (NPP) has been shown to bind glycosaminoglycans and to form a dimer. While these are independent biochemical events, it is likely that dimerization facilitates the interaction with glycosaminoglycans or alternatively, that glycosaminoglycan interaction facilitates the formation of an NPP:NPP dimer. The computer program MODELLER was used to generate a homology model of the collagen α1(XI) NPP monomer using the crystal structure of the closely related noncollagenous-4 (NC4) domain of collagen α1(IX) (PDB:2UUR) as the template. Additionally, a dimer model of collagen α1(XI) NPP domain was created based upon the thrombospondin dimer template (PDB:1Z78). The structure of the dimer created in MODELLER was validated by comparison to a dimer model generated

SUBMITTER: McDougal OM 

PROVIDER: S-EPMC4193664 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature