Lemaitre V, Willbold D, Watts A, Fischer W B
Biomembrane Structure Unit, Department of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK.
J Biomol Struct Dyn. 2006 Apr;23(5):485-96. doi: 10.1080/07391102.2006.10507074.
Based on structures made available by solution NMR, molecular models of the protein Vpu from HIV-1 were built and refined by 6 ns MD simulations in a fully hydrated lipid bilayer. Vpu is an 81 amino acid type I integral membrane protein encoded by the human immunodeficiency virus type-1 (HIV-1) and closely related simian immunodeficiency viruses (SIVs). Its role is to amplify viral release. Upon phosphorylation, the cytoplasmic domain adopts a more compact shape with helices 2 and 3 becoming almost parallel to each other. A loss of helicity for several residues belonging to the helices adjacent to both ends of the loop region containing serines 53 and 57 is observed. A fourth helix, present in one of the NMR-based structures of the cytoplasmic domain and located near the C-terminus, is lost upon phosphorylation.
基于溶液核磁共振提供的结构，在完全水合的脂质双层中通过6纳秒的分子动力学模拟构建并优化了来自HIV-1的蛋白质Vpu的分子模型。Vpu是一种由人类免疫缺陷病毒1型（HIV-1）和密切相关的猴免疫缺陷病毒（SIV）编码的81个氨基酸的I型整合膜蛋白。其作用是增强病毒释放。磷酸化后，细胞质结构域呈现出更紧凑的形状，螺旋2和螺旋3几乎相互平行。观察到属于包含丝氨酸53和57的环区域两端相邻螺旋的几个残基的螺旋度丧失。存在于细胞质结构域的一种基于核磁共振的结构中且位于C末端附近的第四个螺旋在磷酸化后丢失。
