title: NMR assignments and ligand-binding studies on a two-domain family GH19 chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen.
abstract: A two-domain family GH19 chitinase from Japanese cedar (Cryptomeria japonica) pollen, CJP-4, which consists of an N-terminal CBM18 domain and a GH19 catalytic domain, is known to be an important allergen, that causes pollinosis. We report here the resonance assignments of the NMR spectrum of CJP-4. The backbone resonances were almost completely assigned, and the secondary structure was estimated based on the chemical shift values. The addition of a chitin dimer to the enzyme solution perturbed the chemical shifts of the resonances of amino acid residues forming a long extended binding site spanning from the CBM18 domain to the GH19 catalytic domain.
authors.affiliation: Department of Advanced Bioscience, Kindai University, 3327-204, Nakamachi, Nara, 631-8505, Japan.
authors.forename: Tomoya
authors.initials: T
authors.lastname: Takashima
authors.affiliation: Department of Advanced Bioscience, Kindai University, 3327-204, Nakamachi, Nara, 631-8505, Japan.
authors.forename: Takayuki
authors.initials: T
authors.lastname: Ohnuma
authors.affiliation: Department of Advanced Bioscience, Kindai University, 3327-204, Nakamachi, Nara, 631-8505, Japan. fukamizo@nara.kindai.ac.jp.
authors.forename: Tamo
authors.initials: T
authors.lastname: Fukamizo
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000378:metabolism*; D002688:Chitinases / Q000737:chemistry* / Q000378:metabolism*; D032485:Cryptomeria / Q000201:enzymology*; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D000072417:Protein Domains
chemical_list: D000485:Allergens; D008024:Ligands; D002688:Chitinases
keywords: CBM18 domain; Cedar pollen; Cryptomeria japonica; Ligand binding; Secondary structure; Two-domain family GH19 chitinase