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Myosin light chain
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Myosin light chain
A myosin light chain is a light chain (small polypeptide subunit) of myosin. Myosin light chains were discovered by Chinese biochemist Cao Tianqin (Tien-chin Tsao) when he was a graduate student at the University of Cambridge in England.
Structurally, myosin light chains belong to the EF-hand family, a large family of Ca2+- binding proteins. MLCs contain two Ca2+ - binding EF-hand motifs. MLCs isoforms modulate the Ca2+of force transduction and cross-bridge kinetics.
Myosin light chains (MLCs) can be broadly classified into two groups:
Essential and regulatory MLCs have molecular masses of 22 and 19 kDa, respectively. Structurally, MLC2 contains a serine residue that is lacking in MLC1. The presence of this amino acids allows the regulation of the conformational changes (from compacted to an elongated form) by a Ca2+-mediated phosphorylation mechanism. MLC1, in contrast with MLC2, has a N-terminal sequence able to bind actin, contributing to force production.
MLCs are structurally and functionally distinct from myosin heavy chains (MHCs). Nevertheless, the association of MLCs with the neck region of MHCs is necessary for the assembly of the macromolecular complexes that result in the functional motor protein, myosin. The interaction of MLCs with the α-helical neck region of MHC molecule stabilizes the complex .
To this day, eight genes encoding for MLCs in mammalians have been described; several isoforms have also been characterized. Four out of the 8 genes are MLC1 genes, whilst the remaining are MLC2 genes.
MLC1 genes:
MLC2 genes:
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Myosin light chain
A myosin light chain is a light chain (small polypeptide subunit) of myosin. Myosin light chains were discovered by Chinese biochemist Cao Tianqin (Tien-chin Tsao) when he was a graduate student at the University of Cambridge in England.
Structurally, myosin light chains belong to the EF-hand family, a large family of Ca2+- binding proteins. MLCs contain two Ca2+ - binding EF-hand motifs. MLCs isoforms modulate the Ca2+of force transduction and cross-bridge kinetics.
Myosin light chains (MLCs) can be broadly classified into two groups:
Essential and regulatory MLCs have molecular masses of 22 and 19 kDa, respectively. Structurally, MLC2 contains a serine residue that is lacking in MLC1. The presence of this amino acids allows the regulation of the conformational changes (from compacted to an elongated form) by a Ca2+-mediated phosphorylation mechanism. MLC1, in contrast with MLC2, has a N-terminal sequence able to bind actin, contributing to force production.
MLCs are structurally and functionally distinct from myosin heavy chains (MHCs). Nevertheless, the association of MLCs with the neck region of MHCs is necessary for the assembly of the macromolecular complexes that result in the functional motor protein, myosin. The interaction of MLCs with the α-helical neck region of MHC molecule stabilizes the complex .
To this day, eight genes encoding for MLCs in mammalians have been described; several isoforms have also been characterized. Four out of the 8 genes are MLC1 genes, whilst the remaining are MLC2 genes.
MLC1 genes:
MLC2 genes:
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