Collagen domains

Figure 2 Schematic illustration of the varying lengths of the collagenous domains in human collagen types. The collagenous domain is indicated by a yellow-colored box. The noncollagenous domains are indicated as black bars. Some collagen types are processed before integration in their final location within the extracellular matrix.

The type IV collagen molecule is comprised of the N-terminal collagenous 7S domain, which has a sedimentation coefficient of the central major collagenous domain with more than 20 interruptions... 

Type IV collagen subtype [ctl(IV)]2Q 2(IV) from bovine lens capsule forms a fine meshwork structure containing many branches with about 20 nm between the branching points. There are three types of supramolecular assembly of type IV collagen molecules dimer formation (with six polypeptide chains) at the C-terminal NCI domain, the association of four molecules (12 chains) in a 30 nm tetramer formation at the N-terminal 7S domain, and lateral interaction at the collagenous domain (Figure 5(a)). ° ... 

Figure 5 (a) Supramolecular assembly of type IV collagen molecules (1) a dimer formation at the C-terminal NC1 domain, (2) the association of four molecules at the N-terminal 7S domain, and (3) lateral interaction at the collagenous domain. 

Figure 6 Model of type VI collagen assembly. Two type VI collagen molecules assemble with 30 nm overlap " with two pairs of disulfide bonds between cysteines, one in collagenous domain and another in the C-terminal globular domain.Two dimers form a tetramer with disulfide bonds presumably in the a3(VI) chains. The tetramers assemble into the long beaded filamentous structure with 105nm periodicity.

Mutations in both the NC and collagenous domains of COL6A1, COL6A2, or COL6A3 cause Bethlem myopathya dominantly inherited disorder. Ulrich congenital muscular dystrophy can be caused by... 

Type Xn collagen consists of two short collagenous domains COLl and COL2 along with three NC domains (NCI—NC3) (Figure 7) 9 293 N-terminal NC3 domain makes up close to 90% of the total molecular... 

Type XVI collagen is composed of 10 collagenous domains (COLI-COLIO) flanked by 11 NC domains. Type XVI collagen localizes near the dermal-epidermal junction. From immunoelectron microscopy of the papillary dermis, type XVI collagen associates with a fibrillin-1-containing matrix but not on collagen fibrils. ... 

Most types of collagen are extracellular matrix proteins but four of the vertebrate collagens (XIII, XVII, XXIII, and XXV) are classified as type II membrane proteins. They contain an N-terminal cytoplasmic domain, a transmembrane domain, and an extracellular collagenous domain. Also, a membrane-bound protein, ectodys-plasin-A, is a membrane protein with 19 -Gly-Xaa-Yaa- repeat. Macrophage scavenger receptor, ... 

Data shown are the values per 1000 residues of pepsin-resistaht collagenous domain. 

All of the 12 fibril-forming a chains share a long uninterrupted collagenous domain flanked by N- and C-terminal NC propeptides. The a chains assemble into at least 12 type-specific protomers, characterized as homo- and heterotrimers. The chains of fibrillar collagens associate first through a series of noncovalent interactions between the C-terminal NC domains (NCI), which provide correct alignment and registration for... 

Type VIII collagen is composed of highly conserved al(VIII) and a2(VIII) chains, which contain a short collagenous domain of454 residues flanked by an N-terminal NC domain of 117 residues and a C-terminal NC domain of 173 residues." The chains assemble into two distinct homotrimers that assemble into hexagonal lattices. ° The crystal structure of the al C-terminal NC homotrimerization domain was determined (see Section 5.16.6.5). 

Type X collagen has a single al chain, which contains a short collagenous domain of 460 residues, flanked by an N-terminal NC domain of 37 residues and C-terminal NC domain of 161 residues." Its protomer is a homotrimer. The C-terminal NC domain is responsible for trimerization and multimer formation, which is based on experiments with recombinant domains." The crystal structure of type X collagen trimerization domain is similar to that of type VIII collagen (see also Section 5.16.6.5). 

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