3VOW

Crystal Structure of the Human APOBEC3C having HIV-1 Vif-binding Interface

3VOW の概要

• エントリーDOI: 10.2210/pdb3vow/pdb
• 分子名称: Probable DNA dC->dU-editing enzyme APOBEC-3C, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: apobec3c, apobec3, antiviral deffense, host-virus interaction, metal-binding, hiv-1 vif, bet, single domain, sivagm, z2, hydrolase, hiv
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9NRW3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45869.98

構造登録者

Kitamura, S.,Suzuki, A.,Watanabe, N.,Iwatani, Y. (登録日: 2012-02-22, 公開日: 2012-10-03, 最終更新日: 2023-11-08)

主引用文献

Kitamura, S.,Ode, H.,Nakashima, M.,Imahashi, M.,Naganawa, Y.,Kurosawa, T.,Yokomaku, Y.,Yamane, T.,Watanabe, N.,Suzuki, A.,Sugiura, W.,Iwatani, Y.
The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.
Nat.Struct.Mol.Biol., 19:1005-1010, 2012

PubMed Abstract: The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3 (APOBEC3, referred to as A3) proteins are cellular cytidine deaminases that potently restrict retrovirus replication. However, HIV-1 viral infectivity factor (Vif) counteracts the antiviral activity of most A3 proteins by targeting them for proteasomal degradation. To date, the structure of an A3 protein containing a Vif-binding interface has not been solved. Here, we report a high-resolution crystal structure of APOBEC3C and identify the HIV-1 Vif-interaction interface. Extensive structure-guided mutagenesis revealed the role of a shallow cavity composed of hydrophobic or negatively charged residues between the α2 and α3 helices. This region is distant from the DPD motif (residues 128-130) of APOBEC3G that participates in HIV-1 Vif interaction. These findings provide insight into Vif-A3 interactions and could lead to the development of new pharmacologic anti-HIV-1 compounds.

PubMed: 23001005
DOI: 10.1038/nsmb.2378

実験手法

X-RAY DIFFRACTION (2.15 Å)