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4IHK

Crystal structure of the Collagen VI alpha3 N5 domain R1061Q

Summary for 4IHK
Entry DOI10.2210/pdb4ihk/pdb
Related4IGI
DescriptorCollagen alpha3(VI) (2 entities in total)
Functional Keywordscell adhesion, collagen vi 3n5, vwa
Biological sourceMus musculus (mouse)
Total number of polymer chains1
Total formula weight21682.65
Authors
Mikolajek, H.,Becker, A.K.A.,Paulsson, M.,Wagener, R.,Werner, J.M. (deposition date: 2012-12-19, release date: 2013-12-18, Last modification date: 2023-11-08)
Primary citationBecker, 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: 24332716
DOI: 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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