title: Structure of giant muscle proteins.
abstract: Giant muscle proteins (e.g., titin, nebulin, and obscurin) play a seminal role in muscle elasticity, stretch response, and sarcomeric organization. Each giant protein consists of multiple tandem structural domains, usually arranged in a modular fashion spanning 500 kDa to 4 MDa. Although many of the domains are similar in structure, subtle differences create a unique function of each domain. Recent high and low resolution structural and dynamic studies now suggest more nuanced overall protein structures than previously realized. These findings show that atomic structure, interactions between tandem domains, and intrasarcomeric environment all influence the shape, motion, and therefore function of giant proteins. In this article we will review the current understanding of titin, obscurin, and nebulin structure, from the atomic level through the molecular level.
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University Harrisonburg, VA, USA.
authors.forename: Logan C
authors.initials: LC
authors.lastname: Meyer
authors.affiliation: Department of Chemistry and Biochemistry, James Madison University Harrisonburg, VA, USA.
authors.forename: Nathan T
authors.initials: NT
authors.lastname: Wright
keywords: fibronectin type III; immunoglobulin; nebulin; obscurin; structure; titin