Advances in the structural understanding of Vif proteins
Advances in the structural understanding of Vif proteins
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DOI：
10.2174/157016208783885056
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发表时间：
2008-03-01
影响因子：
1
通讯作者：
Tisne, Carine
中科院分区：
文献类型：
--
作者：
Barraud, Pierre;Paillart, Jean-Christophe;Tisne, Carine
多结构域HIV-1 Vif蛋白招募几个细胞伴侣以实现APOBEC 3蛋白的抗病毒活性的中和。Vif主要通过与Cullin 5、ElonginB和ElonginC形成E3泛素连接酶来中和APOBEC 3G和APOBEC 3F，所述E3泛素连接酶靶向这些蛋白质以通过泛素-蛋白酶体途径降解。Vif与Cullin 5-ElonginB-ElonginC复合物通过其SOCS-box基序直接结合ElonginC并通过保守的HCCH基序形成的锌结合区内的疏水残基与Cullin 5结合。HIV-1 Vif-Cullin 5-ElonginBC复合物然后能够通过其N-末端结构域泛素化与Vif结合的APOBEC 3G因子。在这篇综述中，我们总结了目前的知识的结构决定因素的Vif，使其与细胞和病毒的合作伙伴。
The multidomain HIV-1 Vif protein recruits several cellular partners to achieve neutralization of the antiviral activity of APOBEC3 proteins. Vif neutralizes APOBEC3G and APOBEC3F predominantly by forming an E3 ubiquitin ligase with Cullin5, ElonginB and ElonginC that targets these proteins for degradation by the ubiquitin-proteasome pathway. Vif associates with the Cullin5-ElonginB-ElonginC complex by binding directly to ElonginC via its SOCS-box motif and to Cullin5 via hydrophobic residues within a zinc-binding region formed by a conserved HCCH motif. The HIV-1 Vif-Cullin5-ElonginBC complex is then able to ubiquitinate the APOBEC3G factor bound to Vif by its N-terminal domain. In this review, we summarize the current knowledge about the structural determinants of Vif that allow it to interact with cellular and viral partners.