title: H(N), N, C(α), C(β) and C' assignments of the intrinsically disordered C-terminus of human adenosine A2A receptor.
abstract: The C-terminus of the human adenosine A2A receptor differs from the other human adenosine receptors by its exceptional length and lack of a canonical cysteine residue. We have previously structurally characterized this C-terminal domain and its interaction with calmodulin. It was shown to be structurally disordered and flexible, and to bind calmodulin with high affinity in a calcium-dependent manner. Interaction with calmodulin takes place at the N-terminal end of the A2A C-terminal domain without major conformational changes in the latter. NMR was one of the biophysical methods used in the study. Here we present the H(N), N, C(α), C(β) and C' chemical shift assignments of the free form of the C-terminus residues 293-412, used in the NMR spectroscopic characterization of the domain.
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
authors.forename: Helena
authors.initials: H
authors.lastname: Tossavainen
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
authors.forename: Maarit
authors.initials: M
authors.lastname: Hellman
authors.affiliation: Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.|Biocenter Oulu, University of Oulu, Oulu, Finland.
authors.forename: Henni
authors.initials: H
authors.lastname: Piirainen
authors.affiliation: Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.|Biocenter Oulu, University of Oulu, Oulu, Finland.
authors.forename: Veli-Pekka
authors.initials: VP
authors.lastname: Jaakola
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland. Perttu.Permi@helsinki.fi.
authors.forename: Perttu
authors.initials: P
authors.lastname: Permi
mesh_terms: D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011392:Proline / Q000737:chemistry; D043705:Receptor, Adenosine A2A / Q000737:chemistry*
chemical_list: D064267:Intrinsically Disordered Proteins; D043705:Receptor, Adenosine A2A; D011392:Proline
keywords: Adenosine A2A receptor; Intrinsically disordered; NMR; Resonance assignment