Disulfide bonding as a determinant of the molecular composition of types I, II and III procollagen
- 15 June 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 217 (2) , 216-220
- https://doi.org/10.1016/0014-5793(87)80666-x
Abstract
Procollagen molecules have amino-terminal and carboxy-terminal propeptides at the respective ends of the collagenous triple helix. The carboxy-terminal propeptides enhance and direct the association of proα-chains into procollagen molecules, but the mechanism of this registration function is still obscure. A hypothesis concerning the function of disulfide bonding in the assembly of types I, II and III procollagen is put forward here.Keywords
This publication has 12 references indexed in Scilit:
- Identification of disulfide bonds in carboxy-terminal propeptides of human type I procollagenFEBS Letters, 1987
- COOH-terminal propeptides of the major human procollagensJournal of Molecular Biology, 1987
- High Post-translational Modification Levels In Type II Procollagen Are Not A Consequence Of Slow Triple-Helix FormationCollagen and Related Research, 1985
- Molecular cloning and carboxyl-propeptide analysis of human type III procollagenNucleic Acids Research, 1984
- Nucleotide sequences of complementary deoxyribonucleic acids for the pro.alpha.1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolutionBiochemistry, 1983
- Structure of a cDNA for the pro.alpha.2 chain of human type I procollagen. Comparison with chick cDNA for pro.alpha.2(I) identifies structurally conserved features of the protein and the geneBiochemistry, 1983
- Electrostatic influence of local cysteine environments on disulfide exchange kineticsBiochemistry, 1981
- Folding Mechanism of the Triple Helix in Type‐III Collagen and Type‐III pN–CollagenEuropean Journal of Biochemistry, 1980
- Collagen polymorphism: Isolation and partial characterization of α1(I)-trimer molecules in normal human skinArchives of Biochemistry and Biophysics, 1979
- Principles that Govern the Folding of Protein ChainsScience, 1973