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- Glycobiology and Extracellular Matrices
- Boudko, Sergei PRemove Boudko, Sergei P filter
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Keyword
- collagen2
- extracellular matrix2
- Alport syndrome1
- animal evolution1
- AS1
- atomic force microscopy (AFM)1
- basement membrane1
- chloride1
- collagen IV1
- connective tissue1
- crystal structure1
- diabetic nephropathy1
- DN1
- ECM1
- GBM1
- genetic disease1
- glomerular basement membrane1
- Goodpasture's disease1
- GP1
- kinetics1
- LCL1
- loop-crevice-loop1
- NC1 domain1
- protein self-assembly1
- X-ray crystallography1
Glycobiology and Extracellular Matrices
2 Results
- Research ArticleOpen Access
Collagen IVα345 dysfunction in glomerular basement membrane diseases. II. Crystal structure of the α345 hexamer
Journal of Biological ChemistryVol. 296100591Published online: March 25, 2021- Sergei P. Boudko
- Ryan Bauer
- Sergei V. Chetyrkin
- Sergey Ivanov
- Jarrod Smith
- Paul A. Voziyan
- and others
Cited in Scopus: 7Our recent work identified a genetic variant of the α345 hexamer of the collagen IV scaffold that is present in patients with glomerular basement membrane diseases, Goodpasture’s disease (GP) and Alport syndrome (AS), and phenocopies of AS in knock-in mice. To understand the context of this “Zurich” variant, an 8-amino acid appendage, we developed a construct of the WT α345 hexamer using the single-chain NC1 trimer technology, which allowed us to solve a crystal structure of this key connection module. - Glycobiology and Extracellular MatricesOpen Access
A chloride ring is an ancient evolutionary innovation mediating the assembly of the collagen IV scaffold of basement membranes
Journal of Biological ChemistryVol. 294Issue 20p7968–7981Published online: March 28, 2019- Vadim Pedchenko
- Ryan Bauer
- Elena N. Pokidysheva
- Alaa Al-Shaer
- Nancy R. Forde
- Aaron L. Fidler
- and others
Cited in Scopus: 9Collagen IV scaffold is a principal component of the basement membrane (BM), a specialized extracellular matrix that is essential for animal multicellularity and tissue evolution. Scaffold assembly begins with the trimerization of α-chains into protomers inside the cell, which then are secreted and undergo oligomerization outside the cell. For the ubiquitous scaffold composed of α1- and α2-chains, both intracellular and extracellular stages are mediated by the noncollagenous domain (NC1). The association of protomers is chloride-dependent, whereby chloride ions induce interactions of the protomers’ trimeric NC1 domains leading to NC1 hexamer formation.