4IGI
Crystal structure of the Collagen VI alpha3 N5 domain
Summary for 4IGI
| Entry DOI | 10.2210/pdb4igi/pdb |
| Descriptor | Collagen alpha3(VI) (2 entities in total) |
| Functional Keywords | cell adhesion, collagen vi 3n5 |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 21711.71 |
| Authors | Mikolajek, H.,Becker, A.K.A.,Paulsson, M.,Wagener, R.,Werner, J.M. (deposition date: 2012-12-17, release date: 2013-12-18, Last modification date: 2023-11-08) |
| Primary citation | Becker, A.K.,Mikolajek, H.,Paulsson, M.,Wagener, R.,Werner, J.M. A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein Structure, 22:199-208, 2014 Cited by PubMed Abstract: Von Willebrand factor A (VWA) domains are versatile protein interaction domains with N and C termini in close proximity placing spatial constraints on overall protein structure. The 1.2 Å crystal structures of a collagen VI VWA domain and a disease-causing point mutant show C-terminal extensions that place the N and C termini at opposite ends. This allows a "beads-on-a-string" arrangement of multiple VWA domains as observed for ten N-terminal domains of the collagen VI α3 chain. The extension is linked to the core domain by a salt bridge and two hydrophobic patches. Comparison of the wild-type and a muscular dystrophy-associated mutant structure identifies a potential perturbation of a protein interaction interface and indeed, the secretion of mutant collagen VI tetramers is affected. Homology modeling is used to locate a number of disease-associated mutations and analyze their structural impact, which will allow mechanistic analysis of collagen-VI-associated muscular dystrophy phenotypes. PubMed: 24332716DOI: 10.1016/j.str.2013.06.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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