title: The hinge region of type VII collagen is intrinsically disordered.
abstract: Type VII collagen (Col7) is important for skin integrity. As a major component of the anchoring fibrils, Col7 is essential for linking different skin layers together. The central collagenous domain of Col7 contains several interruptions of the collagen triple helix. The longest interruption is 39 amino acids long and referred to as the hinge region. The hinge region is highly conserved between species. This region was predicted to adopt a coiled coil structure and to serve as the trimerization domain of Col7. To gain insight into the potential function of the hinge region we investigated a heterologous expressed peptide by CD and NMR spectroscopy. CD spectroscopy implies that the hinge region is intrinsically disordered. Resonance assignment was performed and allowed secondary structure analysis based on the chemical shift values. Seven amino acids in the N-terminal moiety show residual α-helical conformation. Subsequent investigation of temperature dependency of amide chemical shifts indicated participation in hydrogen bonding of amino acid residues in the C-terminal moiety of the hinge region. Therefore, the hinge region does not form a coiled coil structure under the employed experimental conditions. The intrinsic disorder of the hinge region might be desired for flexibility to serve as a "hinge" or the hinge region is an important interaction site as typically observed for intrinsically disordered proteins.
authors.affiliation: Institute of Chemistry, University of Lübeck, 23538 Lübeck, Germany.
authors.forename: Barbara Christine
authors.initials: BC
authors.lastname: Richer
authors.affiliation: Institute of Chemistry, University of Lübeck, 23538 Lübeck, Germany. Electronic address: karsten.seeger@chemie.uni-luebeck.de.
authors.forename: Karsten
authors.initials: K
authors.lastname: Seeger
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D024143:Collagen Type VII / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D010802:Phylogeny; D020641:Polymorphism, Single Nucleotide; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D024143:Collagen Type VII
keywords: Extracellular matrix; Hinge; Intrinsically disordered protein; NMR; Type VII collagen