Procollagen (Type I) contains a noncollagenous COOH-terminal propeptide (C-propeptide) hypothesized to be important in directing chain association and alignment during assembly. We previously expressed human pro-␣2(I) cDNA in rat liver epithelial cells, W8, that produce only pro-␣1(I) trimer collage
Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis
✍ Scribed by Donald L. Helseth Jr.; Joseph H. Lechner; Arthur Veis
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 624 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The amino‐terminal telopeptide of the collagen α1(I) chain has a highly conserved sequence. This sequence was analyzed by the Chou‐Fasman criteria, and a folded β‐sheet conformation, including a β‐turn, was predicted. This folded “hairpin” region favors both ionic and hydrophobic intermolecular interactions with α1(I) chain residues 930–938 on a neighboring, end‐overlapped molecule. An end‐overlap interaction of this nature could direct the initial step in fibril formation. The predicted structure also places the potential crosslink‐forming lysyl residue, 9^N^, in a unique site at the β‐turn end of the telopeptide.
📜 SIMILAR VOLUMES
Collagen biosynthesis is a complex process that begins with the association of three procollagen chains. A series of conserved intra-and interchain disulfide bonds in the carboxyl-terminal region of the procollagen chains, or C-propeptide, has been hypothesized to play an important role in the nucle
Evidence from a variety of sources indicates that the extracellular matrix forms an important part of a feedback loop governing the migration, proliferation, and differentiation of the cells that produce it. In keeping with this, we showed previously that the extracellular matrix of a multipotential
A young girl presented with severe type 111 osteogenesis imperfecta; her otherwise healthy mother also had a mild connective tissue disorder with blue sclerae and recurrent joint dislocations. Skin fibroblast cultures from the child produced both normal and post-translationally overmodified type I c