Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon
- PMID: 12623021
- DOI: 10.1016/s0969-2126(03)00025-x
Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon
Abstract
In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
Similar articles
-
Stabilization of short collagen-like triple helices by protein engineering.J Mol Biol. 2001 May 18;308(5):1081-9. doi: 10.1006/jmbi.2001.4644. J Mol Biol. 2001. PMID: 11352592
-
Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from third to first order kinetics.J Mol Biol. 2002 Mar 29;317(3):459-70. doi: 10.1006/jmbi.2002.5439. J Mol Biol. 2002. PMID: 11922677
-
Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.J Mol Biol. 2004 Sep 3;342(1):219-27. doi: 10.1016/j.jmb.2004.07.008. J Mol Biol. 2004. PMID: 15313619
-
Triple-helical peptides: an approach to collagen conformation, stability, and self-association.Biopolymers. 2008 May;89(5):345-53. doi: 10.1002/bip.20958. Biopolymers. 2008. PMID: 18275087 Review.
-
Revisiting the molecular structure of collagen.Connect Tissue Res. 2008;49(5):299-310. doi: 10.1080/03008200802325110. Connect Tissue Res. 2008. PMID: 18991083 Review.
Cited by
-
Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency.Biomacromolecules. 2022 Sep 12;23(9):3507-3516. doi: 10.1021/acs.biomac.2c00170. Epub 2022 Aug 11. Biomacromolecules. 2022. PMID: 35952369 Free PMC article.
-
A tale of two symmetrical tails: structural and functional characteristics of palindromes in proteins.BMC Bioinformatics. 2008 Jun 11;9:274. doi: 10.1186/1471-2105-9-274. BMC Bioinformatics. 2008. PMID: 18547401 Free PMC article.
-
Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.J Am Chem Soc. 2011 Feb 16;133(6):1686-9. doi: 10.1021/ja109972p. Epub 2011 Jan 19. J Am Chem Soc. 2011. PMID: 21247159 Free PMC article.
-
Structural characterization of a beta-turn mimic within a protein-protein interface.Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18336-41. doi: 10.1073/pnas.1004187107. Epub 2010 Oct 11. Proc Natl Acad Sci U S A. 2010. PMID: 20937907 Free PMC article.
-
Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis.J Exp Med. 2009 Feb 16;206(2):449-62. doi: 10.1084/jem.20081862. Epub 2009 Feb 9. J Exp Med. 2009. PMID: 19204106 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
