Chemical shift assignments for the Ig2 domain of human obscurin A.
Biomol NMR Assign
; 10(1): 63-5, 2016 Apr.
Article
em En
| MEDLINE
| ID: mdl-26373426
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ressonância Magnética Nuclear Biomolecular
/
Fatores de Troca de Nucleotídeo Guanina Rho
Limite:
Humans
Idioma:
En
Revista:
Biomol NMR Assign
Ano de publicação:
2016
Tipo de documento:
Article