Biomaterial Database

The NC1 domain of human collagen IV is necessary to initiate triple helix formation. 2004

Stephan Söder, and Ernst Pöschl

Osteoarticular and Arthritis Research, Department of Pathology, University of Erlangen-Nürnberg, Germany. stephan.soeder@patho.imed.uni-erlangen.de

Type IV collagen is a heterotrimeric molecule, which contains the N-terminal 7S, a central triple-helical domain, and the globular C-terminal NC1 domain. A zipper-like mechanism of triple helix formation, starting from the C-terminus, has been proposed for most collagens but for collagen type IV there has only been indirect evidence so far. In this study we expressed trimeric human collagen type IV to compare the effects of different structural variants on the formation of collagen IV molecules. Our data show that the NC1 but not 7S domain is essential for the chain association and initiation of triple helix formation. This strongly suggests an N-to-C terminal mechanism of triple helix formation. Additionally, we could show that the human alpha2(IV) chain can form chimeric alpha1.alpha1.alpha2(IV) heterotrimers with mouse subunits when expressed in PF-HR9 cells.

UI	MeSH Term	Description	Entries
D011994	Recombinant Proteins	Proteins prepared by recombinant DNA technology.	Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002460	Cell Line	Established cell cultures that have the potential to propagate indefinitely.	Cell Lines,Line, Cell,Lines, Cell
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D017433	Protein Structure, Secondary	The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation.	Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D017434	Protein Structure, Tertiary	The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.	Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D051379	Mice	The common name for the genus Mus.	Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus
D020836	Protein Structure, Quaternary	The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).	Quaternary Protein Structure,Protein Structures, Quaternary,Quaternary Protein Structures
D021122	Protein Subunits	Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.	Protomers,Protein Subunit,Protomer,Subunit, Protein,Subunits, Protein
D024141	Collagen Type IV	A non-fibrillar collagen found in the structure of BASEMENT MEMBRANE. Collagen type IV molecules assemble to form a sheet-like network which is involved in maintaining the structural integrity of basement membranes. The predominant form of the protein is comprised of two alpha1(IV) subunits and one alpha2(IV) subunit, however, at least six different alpha subunits can be incorporated into the heterotrimer.	7S Collagen,Collagen Type IV, alpha1 Chain,Collagen Type IV, alpha1 Subunit,Collagen Type IV, alpha2 Chain,Collagen Type IV, alpha2 Subunit,Collagen alpha1(IV),Procollagen Type IV,Type IV (Basement Membrane) Collagen,Type IV Collagen,Type IV Procollagen,alpha1(IV) collagen,Collagen, 7S,Collagen, Type IV,Procollagen, Type IV