要吐了... - 泰坦之旅吧

level 11

ssy_st1991 楼主

The E2–E1 heterodimers form 80 trimeric spikes on the icosahedral virus surface1,2, 60 with quasi-three-fold symmetry and 20 coincident with the icosahedral three-fold axes arranged with T=4 quasi-symmetry.
The lower pH in the endosome induces the virions to undergo an irreversible conformational change in which E2 and E1 dissociate and E1 forms homotrimers,triggering fusion of the viral membrane with the endosomal membrane and then releasing the viral genome into the cytoplasm.
The X-ray crystal structure of the ectodomain of the E1 protein(residues 1–383)from Semliki Forest virus (SFV) is homologous to the flavivirus E glycoprotein and consists of three b-barrel domains(domains I, II and III; notated as DI, DII and DIII) with the fusion loop at the distal end of DII.
However, other residues that were associated with cell recognition are in the disordered domain B showing that there could be several sites on the virus surface that associate with various cell surface molecules involved in virus attachment and entry.
The A domains of the three E2 molecules within one trimeric spike
are situated in the centre of the triangular cavity formed by the three E1
molecules in the spike andmake extensive interactions with each other
在翻译这堆破玩意之前真特么没见过这么长的句子啊，中间一个停顿没有，看到后面那个句子的时候真特么差点吐出来... [瀑布汗~]