ZAP 氨基端结构域的结构表明锌指蛋白如何识别复杂的 RNA。
Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA.
机构信息
State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
出版信息
Nat Struct Mol Biol. 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243.
Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. How ZAP recognizes its target RNA has been unclear. Here we report the crystal structure of the N-terminal domain of rat ZAP (NZAP225), the major functional domain. The overall structure of NZAP225 resembles a tractor, with four zinc-finger motifs located at the bottom. Structural and functional analyses identified multiple positively charged residues and two putative RNA-binding cavities forming a large putative RNA-binding cleft. ZAP molecules interact to form a dimer that binds to a ZAP-responsive RNA molecule containing two ZAP-binding modules. These results provide insights into how ZAP binds specifically to complex target RNA.
锌指抗病毒蛋白（ZAP）是一种宿主因子，通过靶向病毒 mRNA 进行降解，特异性抑制某些病毒（如 HIV-1）的复制。ZAP 如何识别其靶 RNA 尚不清楚。本文报道了大鼠 ZAP（NZAP225）的 N 端结构域（主要功能域）的晶体结构。NZAP225 的整体结构类似于拖拉机，底部有四个锌指基序。结构和功能分析确定了多个带正电荷的残基和两个可能的 RNA 结合腔，形成了一个大的可能的 RNA 结合裂隙。ZAP 分子相互作用形成二聚体，与含有两个 ZAP 结合模块的 ZAP 反应性 RNA 分子结合。这些结果提供了 ZAP 如何特异性结合复杂靶 RNA 的见解。
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