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hanbing7525银虫 (小有名气)
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[求助]
帮忙翻译，英译汉
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| C3c is an inactive, terminal fragment released from iC3b by the factor I protease (Fig. 1A). The C3c crystal structure demonstrates marked rearrangements compared with C3 in the MG7 and MG8 domains, lesser movements in the MG2, MG3, and MG6 domains that abut MG7 and MG8, and reorientation of the C345C domain (12) (Fig. 1B). Most remarkably, the 19-residue NT ( N-terminal) segment, which becomes Nterminal in the -chain after removal of C3a (Fig. 1A), moves from the MG3/MG8 side of the key ring in C3 to the MG7 side in C3c, by slipping between the MG1–4 ring and MG5–6 half-ring at its C-terminal connection to MG6 (12). EM averages of C3c clearly revealed the MG domain key ring and the C345C knob (Fig. 2B) and correlated excellently with the C3c crystal structure (Fig. 3 D and E). Orientations of C3c with the MG1–4 ring in front or back can clearly be distinguished by the orientation of the C345C knob and the weak density of the key ring where it is only a single MG domain thick at MG4 (compare Dand E in Fig. 3). These features enable the orientation of the C3c moiety within the fragments described below to be assessed even without reference to cross-correlations. |
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