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TPM2
β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the ''TPM2'' gene.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7169 )〕 β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.
== Structure ==
β-tropomyosin is roughly 32 kDa in molecular weight (284 amino acids), but multiple splice variants exist.〔(【引用サイトリンク】url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P07951 )〕〔(【引用サイトリンク】url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P07951-2 )〕〔(【引用サイトリンク】url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P07951-3 )〕 Tropomysin is a flexible protein homodimer or heterodimer composed of two alpha-helical chains, which adopt a bent coiled coil conformation to wrap around the seven actin molecules in a functional unit of muscle. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. Tropomyosin dimers are composed of varying combinations of tropomyosin isoforms; human striated muscles express protein from the ''TPM1'' (α-tropoomyosin), ''TPM2'' (β-tropomyosin) and ''TPM3'' (γ-tropomyosin) genes, with α-tropomyosin being the predominant isoform in striated muscle. Fast skeletal muscle and cardiac muscle contain more αα-homodimers, and slow skeletal muscle contains more ββ-homodimers. In human cardiac muscle the ratio of α-tropomyosin to β-tropomyosin is roughly 5:1. It has been shown that different combinations of tropomyosin isoforms bind troponin T with differing affinities, demonstrating that isoform combinations are used to impart a specific functional impact.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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