Backbone (15)N relaxation analysis of the N-terminal domain of the HTLV-I capsid protein and comparison with the capsid protein of HIV-1.
Backbone (15)N relaxation analysis of the N-terminal domain of the HTLV-I capsid protein and comparison with the capsid protein of HIV-1.
复制标题
HTLV-I 衣壳蛋白 N 末端结构域的主链 (15)N 松弛分析以及与 HIV-1 衣壳蛋白的比较。
DOI：
10.1110/ps.0235903
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Tjandra,Nico
中科院分区：
文献类型：
--
作者：
Cornilescu,ClaudiaC;Bouamr,Fadila;Carter,Carol;Tjandra,Nico
Recently we published a structural study of the N-terminal domain of the retroviral capsid (CA) protein from the human T-cell leukemia virus type I (HTLV-I; Cornilescu et al. 2001), an oncogenic retrovirus with tropism for T-cells.Despite the low sequence conservation in the N-terminal domain (NTD), the mostly helical structure is highly similar among different retroviral capsid NTDs. The N-terminal 134-amino-acid fragment (CA134) contains a central sixhelix core packed through (extensive) hydrophobic contacts and a ß-hairpin. The potential to form an N-terminal Pro 1–Asp (Glu) salt bridge that links Asp (Glu) in the helical core to the N terminus to form the ß-hairpin is highly conserved in the retroviral family. In all mature retrovirus particles, the CA protein forms the shell of an inner core structure that encases the diploid RNA genome and the replicative enzymes. Whereas the noninfectious, immature particles look alike in the electron microscope, the mature particles are morphologically distinct and are characterized by the shape of the capsid core structure. The mature virion of HIV-1 and other lentiviruses is conical, spherical for HTLV-I, and an irregular polyhe-
