Structural highlights
Function
[COFA1_HUMAN] Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.[1] Restin potently inhibits angiogenesis.
Publication Abstract from PubMed
Correct folding of the collagen triple helix requires a self-association step which selects and binds alpha-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four beta-sheets and an alpha-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by beta-sheet planes from each monomer. The trimerization domain is extremely stable and forms at picomolar concentrations. It is found that the trimerization domain of type XV collagen is structurally similar to that of type XVIII, despite only 32% sequence identity. High structural conservation indicates that the multiplexin trimerization domain represents a three dimensional fold that allows for sequence variability while retaining structural integrity necessary for tight and efficient trimerization.
Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens.,Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bachinger HP Matrix Biol. 2010 Oct 12. PMID:20932905[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramchandran R, Dhanabal M, Volk R, Waterman MJ, Segal M, Lu H, Knebelmann B, Sukhatme VP. Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin. Biochem Biophys Res Commun. 1999 Feb 24;255(3):735-9. PMID:10049780 doi:http://dx.doi.org/10.1006/bbrc.1999.0248
- ↑ Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bachinger HP. Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens. Matrix Biol. 2010 Oct 12. PMID:20932905 doi:10.1016/j.matbio.2010.09.005
