title: Chemical shift assignments of the connexin37 carboxyl terminal domain.
abstract: Connexin37 (Cx37) is a gap junction protein involved in cell-to-cell communication in the vasculature and other tissues. Cx37 suppresses proliferation of vascular cells involved in tissue development and repair in vivo, as well as tumor cells. Global deletion of Cx37 in mice leads to enhanced vasculogenesis in development, as well as collateralgenesis and angiogenesis in response to injury, which together support improved tissue remodeling and recovery following ischemic injury. Here we report the1H,15N, and13C resonance assignments for an important regulatory domain of Cx37, the carboxyl terminus (CT; C233-V333). The predicted secondary structure of the Cx37CT domain based on the chemical shifts is that of an intrinsically disordered protein. In the1H-15N HSQC, N-terminal residues S254-Y259 displayed a second weaker peak and residues E261-Y266 had significant line broadening. These residues are flanked by prolines (P250, P258, P260, and P268), suggesting proline cis-trans isomerization. Overall, these assignments will be useful for identifying the binding sites for intra- and inter-molecular interactions that affect Cx37 channel activity.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, 68198, USA.
authors.forename: Hanjun
authors.initials: H
authors.lastname: Li
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, 68198, USA.
authors.forename: Gaelle
authors.initials: G
authors.lastname: Spagnol
authors.affiliation: Department of Physiology, University of Arizona, Tucson, AZ, USA.
authors.forename: Tasha K
authors.initials: TK
authors.lastname: Pontifex
authors.affiliation: Department of Physiology, University of Arizona, Tucson, AZ, USA.
authors.forename: Janis M
authors.initials: JM
authors.lastname: Burt
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, 68198, USA. psorgen@unmc.edu.
authors.forename: Paul L
authors.identifier: http://orcid.org/0000-0002-7766-2083
authors.initials: PL
authors.lastname: Sorgen
mesh_terms: D000818:Animals; D017630:Connexins / Q000737:chemistry*; D051379:Mice; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D000097006:Gap Junction alpha-4 Protein
chemical_list: D017630:Connexins; D000097006:Gap Junction alpha-4 Protein
keywords: Carboxyl terminus; Cx37; Gap junction; Intrinsically disordered protein