本帖最后由 细胞海洋 于 2012-10-12 21:40 编辑 " B' d0 i, T% a$ e # }- N9 ]' p+ z% d# k) N7 \3 b2 u[attach]46579[/attach]0 `, o4 V0 @4 q- Y
12 October, 2012 Volume 151, Issue 29 H. D6 `. K* X" o- Q
On the cover: Adenovirus, which causes the common cold, has evolved small oncoproteins that hijack human cells by inactivating tumor suppressors. In this issue, Ou et al. (pp. 304–319) address a longstanding question: what is the structural basis for the multiple dominant interactions of small Adenovirus oncoproteins? E4-ORF3 is a 13 kDa oncoprotein that inactivates p53, PML, TRIM24, and MRN. Structural analysis of E4-ORF3 reveals that it self-assembles to create a nonrepeating polymer that has binding sites capable of trapping cellular tumor suppressor complexes. The cover shows the E4-ORF3 avidity matrix (yellow) in the nucleus (nuclear membrane shown in blue) of an infected human cell, where it physically partitions viral DNA replication centers (red) from cellular chromatin (nucleoli, green). Image credit: Andrew Noske and Tom Deerinck.' F7 J0 X" B5 R 作者: ljs 时间: 2012-10-12 22:10
