title: Molecular basis of organization of collagen fibrils.
abstract: The collagen fibrils are formed by self-assembly of individual collagen molecules, but the mechanism that drives their orderly packing during fibril formation is not clearly defined. To identify structural determinants critical for the D-periodic alignment of collagen molecules we employed three sets of genetically engineered collagen II variants: (i) a set in which domains corresponding to the specific D periods have been purposely deleted, (ii) a set of collagen variants consisting of tandem repeats of a specific D period, and (iii) a set lacking definite fragments of the D4 period. All collagen variants were analyzed for their ability to assemble into D-periodic fibrils. Even though all genetically engineered collagen variants differ significantly from the wild-type collagen II, most of them were able to form filamentous structures. The D-periodic banding pattern, an indication of the staggered arrangement of collagen monomers, however, occurred only when the D1, D4, and D0.4 domains of interacting collagen monomers could potentially cluster together to form a triad through telopeptide-mediated binding. Our results identify a critical step in the formation of collagenous matrices and provide experimental evidence for the active involvement of the N-terminal and C-terminal regions of fibrillar collagens in this process.
authors.affiliation: Department of Dermatology and Cutaneous Biology, Jefferson Medical College, and Jefferson Institute of Molecular Medicine, Thomas Jefferson University, BLSB, Room 424, 233 S. 10th Street, Philadelphia, PA 19107, USA.
authors.forename: Andrzej
authors.initials: A
authors.lastname: Steplewski
authors.forename: Vera
authors.initials: V
authors.lastname: Hintze
authors.forename: Andrzej
authors.initials: A
authors.lastname: Fertala
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D024043:Collagen Type II / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D020894:Microfibrils / Q000737:chemistry*; D008954:Models, Biological; D011108:Polymers / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D000596:Amino Acids; D024043:Collagen Type II; D011108:Polymers; D011994:Recombinant Proteins