» Articles » PMID: 18845531

Trimerization and Triple Helix Stabilization of the Collagen XIX NC2 Domain

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2008 Oct 11
PMID 18845531
Citations 18
Authors
Affiliations
Soon will be listed here.
Abstract

The mechanisms of chain selection and assembly of fibril-associated collagens with interrupted triple helices (FACITs) must differ from that of fibrillar collagens, since they lack the characteristic C-propeptide. We analyzed two carboxyl-terminal noncollagenous domains, NC2 and NC1, of collagen XIX as potential trimerization units and found that NC2 forms a stable trimer and substantially stabilizes a collagen triple helix attached to either end. In contrast, the NC1 domain requires formation of an adjacent collagen triple helix to form interchain disulfide bridges. The NC2 domain of collagen XIX and probably of other FACITs is responsible for chain selection and trimerization.

Citing Articles

Collagen formation, function and role in kidney disease.

De Gregorio V, Barua M, Lennon R Nat Rev Nephrol. 2024; 21(3):200-215.

PMID: 39548215 DOI: 10.1038/s41581-024-00902-5.


Abnormalities in esophageal smooth muscle induced by mutations in collagen XIX.

Sato H, Jin K, Yano S, Yasuda A, Adachi S, Yoshioka H Histochem Cell Biol. 2022; 157(2):205-216.

PMID: 34993640 DOI: 10.1007/s00418-021-02059-9.


Type XIX collagen: a promising biomarker from the basement membranes.

Calvo A, Moreno L, Moreno L, Toivonen J, Manzano R, Molina N Neural Regen Res. 2019; 15(6):988-995.

PMID: 31823868 PMC: 7034273. DOI: 10.4103/1673-5374.270299.


Transcriptome profiling reveals transcriptional and alternative splicing regulation in the early embryonic development of hair follicles in the cashmere goat.

Zhang Y, Wang L, Li Z, Chen D, Han W, Wu Z Sci Rep. 2019; 9(1):17735.

PMID: 31780728 PMC: 6882815. DOI: 10.1038/s41598-019-54315-7.


Reversible Covalent End-Capping of Collagen Model Peptides.

Priem C, Geyer A Chemistry. 2019; 25(63):14278-14283.

PMID: 31557356 PMC: 6900188. DOI: 10.1002/chem.201903460.


References
1.
Frank S, Kammerer R, Mechling D, Schulthess T, Landwehr R, Bann J . Stabilization of short collagen-like triple helices by protein engineering. J Mol Biol. 2001; 308(5):1081-9. DOI: 10.1006/jmbi.2001.4644. View

2.
Jaalinoja J, Ylostalo J, Beckett W, Hulmes D, Ala-Kokko L . Trimerization of collagen IX alpha-chains does not require the presence of the COL1 and NC1 domains. Biochem J. 2007; 409(2):545-54. DOI: 10.1042/BJ20070984. View

3.
Frank S, Boudko S, Mizuno K, Schulthess T, Engel J, Bachinger H . Collagen triple helix formation can be nucleated at either end. J Biol Chem. 2003; 278(10):7747-50. DOI: 10.1074/jbc.C200698200. View

4.
Mechling D, Bachinger H . The collagen-like peptide (GER)15GPCCG forms pH-dependent covalently linked triple helical trimers. J Biol Chem. 2000; 275(19):14532-6. DOI: 10.1074/jbc.275.19.14532. View

5.
Engel J, Bachinger H . Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Matrix Biol. 2000; 19(3):235-44. DOI: 10.1016/s0945-053x(00)00071-8. View