Case Study: Titin Ig domains
نویسندگان
چکیده
In the extreme sport of bungee jumping, a daring athlete leaps from a great height and freefalls while a tethered cord tightens and stretches to absorb the energy from the descent. The bungee cord protects the jumper from serious injury, because its elasticity allows it to extend and provide a cushioning force that opposes gravity during the fall. Amazingly, nature also uses elasticity to dampen biological forces at the molecular level, such as during extension of a muscle fiber under stress. The molecular bungee cord that serves this purpose in the human muscle fiber is the protein titin, which functions to protect muscle fibers from damage due to overstretching. In this case study, we will examine how experimental and theoretical studies yield insight into the molecular mechanism for titin’s elasticity.
منابع مشابه
Properties of titin immunoglobulin and fibronectin-3 domains.
Immunoglobulin (Ig) and fibronectin-3 (Fn3) domains are common building blocks of many extracellular proteins involved in ligand recognition and cell adhesion. Ig and Fn3 domains are also the main components of a group of intracellular proteins associated with the contractile apparatus of muscles. The largest of the intracellular group is titin ( 3 MDa), which has key roles in the assembly and ...
متن کاملStructural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.
BACKGROUND The giant muscle protein titin contributes to the filament system in skeletal and cardiac muscle cells by connecting the Z disk and the central M line of the sarcomere. One of the physiological functions of titin is to act as a passive spring in the sarcomere, which is achieved by the elastic properties of its central I band region. Titin contains about 300 domains of which more than...
متن کاملUnfolding of titin immunoglobulin domains by steered molecular dynamics simulation.
Titin, a 1-microm-long protein found in striated muscle myofibrils, possesses unique elastic and extensibility properties in its I-band region, which is largely composed of a PEVK region (70% proline, glutamic acid, valine, and lysine residue) and seven-strand beta-sandwich immunoglobulin-like (Ig) domains. The behavior of titin as a multistage entropic spring has been shown in atomic force mic...
متن کاملSecondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.
The giant protein titin, which is responsible for passive elasticity in muscle fibers, is built from approximately 300 regular immunoglobulin-like (Ig) domains and FN-III repeats. While the soft elasticity derived from its entropic regions, as well as the stiff mechanical resistance derived from the unfolding of the secondary structure elements of Ig- and FN-III domains have been studied extens...
متن کاملCrystallography of Biological Macromolecules
C218 located at the interface between A-band and M-line. It has been shown by Centner et al. [2] that MURF-1, a member of the RING finger proteins, binds to the two Ig-domains A168 and A169 in proximity to the kinase. Thus, its binding might be involved in the regulation of titin kinase. The structure of this tandem Ig domain has been solved. Ig domains, also in titin, are involved in many prot...
متن کاملStretching molecular springs: elasticity of titin filaments in vertebrate striated muscle.
Titin, the giant protein of striated muscle, provides a continuous link between the Z-disk and the M-line of a sarcomere. The elastic I-band section of titin comprises two main structural elements, stretches of immunoglobulin-like domains and a unique sequence, the PEVK segment. Both elements contribute to the extensibility and passive force development of nonactivated muscle. Extensibility of ...
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