title: Chemical shift assignments for the Ig2 domain of human obscurin A.
abstract: The giant sarcomeric protein obscurin (~720 kDa) is an essential contributor to myofibrillogenesis and acts as the only known tether between the contractile apparatus and the surrounding membrane structures in myofibrils. Genomic characterization of OBSCN suggests a modular architecture, consisting of dozens of individually-folded Ig-like and FnIII-like domains arranged in tandem. Here we describe the sequence-specific chemical shift assignments of the second putative obscurin Ig-like domain (Ig2). This domain specifically binds to MyBP-C slow variant-1 through an unknown mechanism. Ultimately, the assignments presented here will facilitate high-resolution structure determination of Ig2 and provide insight into the specificity of the obscurin-MyBP-C interaction.
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA.
authors.forename: Joshua E
authors.initials: JE
authors.lastname: Temple
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA.
authors.forename: Matthew C
authors.initials: MC
authors.lastname: Oehler
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University, 901 Carrier Dr., Harrisonburg, VA, 22807, USA. wrightnt@jmu.edu.
authors.forename: Nathan T
authors.initials: NT
authors.lastname: Wright
mesh_terms: D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D017346:Protein Serine-Threonine Kinases; D064067:Rho Guanine Nucleotide Exchange Factors / Q000737:chemistry*
chemical_list: D064067:Rho Guanine Nucleotide Exchange Factors; C578224:OBSCN protein, human; D017346:Protein Serine-Threonine Kinases
keywords: MyBP-C slow variant 1; Myogenesis; NMR chemical shift assignments; Obscurin