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The X-ray crystal structure of human myoferlin C2A with a resolution of 1.9 Å is presented, bound to two divalent cations. We also compare its three-dimensional structure and membrane binding activities with C2A dysferlin. Our research findings indicate that, while C2A dysferlin binds to membranes in a Ca2+-dependent manner
read morekeyboard_double_arrow_rightSwisscows
The X-ray crystal structure of human myoferlin C2A, with a resolution of 1.9 Å and bound to two divalent cations, is showcased. We also conduct a comparison between its three-dimensional structure and membrane binding activities with C2A dysferlin. Our research findings suggest that, whereas C2A dysferlin binds to membranes in a Ca2+-dependent manner
read morekeyboard_double_arrow_rightYahoo
The X-ray crystal structure of human myoferlin C2A, with a resolution of 1.9 Å and bound to two divalent cations, is presented. We also compare its three-dimensional structure and membrane binding activities with C2A dysferlin. Our research findings indicate that, while C2A dysferlin binds to membranes in a Ca2+-dependent manner,
read morekeyboard_double_arrow_rightDuckduckgo
The X-ray crystal structure of human myoferlin C2A, with a resolution of 1.9 Å and bound to two divalent cations, is revealed. Additionally, we analyze its three-dimensional structure and membrane binding activities in comparison with C2A dysferlin. Our research findings suggest that, unlike C2A dysferlin, which binds to membranes in a Ca2+-dependent manner
read morekeyboard_double_arrow_right