Structural Basis of Muscle Regulation by Synchrotron X-ray Diffraction— Head-Head Interactions of Myosin Crossbridges in Resting Higher Vertebrate Striated Muscle

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  • OSHIMA Kanji
    Research Associate, Research Center for State-of-the-Art Functional Protein Analysis, Institute for Protein Research, Osaka University
  • WAKABAYASHI Katsuzo
    Graduate School of Engineering Science, Osaka University

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Other Title
  • 放射光X線回折によるミオシンクロスブリッジの頭部間相互作用—ミオシンフィラメントの筋収縮制御の構造的基盤
  • 放射光X線回折によるミオシンクロスブリッジの頭部間相互作用 : ミオシンフィラメントの筋収縮制御の構造的基盤
  • ホウシャコウ Xセン カイセツ ニ ヨル ミオシンクロスブリッジ ノ トウブ カン ソウゴ サヨウ : ミオシンフィラメント ノ キンシュウシュク セイギョ ノ コウゾウテキ キバン

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Skeletal muscle contraction is regulated mainly by Ca2+ binding to the thin actin filaments in a sarcomere, but the participation of the thick myosin filament in the regulatory mechanism has remained to be clarified. The lattice sampling-free intensities of the myosin layer lines in the X-ray diffraction patterns from live resting higher vertebrate striated muscles with a full thick-thin filament overlap were analyzed. Atomic modeling of the myosin filament was performed, revealing the head-head interactions of myosin crossbridges, which are in common among various resting striated muscles. The head-head interactions are primarily electrostatic and the converter domain is responsible for their interactions. The results indicate that multiple head-head interactions of myosin crossbridges stabilize the resting myosin structure and play a role in the regulatory function also in the thin filament-regulated muscles.

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