Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments
2016-06-17
发表期刊JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
卷号291期号:25页码:13098-13112
发表状态已发表
DOI10.1074/jbc.M116.720557
摘要We present the results of solid state nuclear magnetic resonance (NMR) experiments on HIV-1 capsid protein (CA) assemblies with three different morphologies, namely wild-type CA (WT-CA) tubes with 35-60 nm diameters, planar sheets formed by the Arg(18)-Leu mutant (R18L-CA), and R18L-CA spheres with 20-100 nm diameters. The experiments are intended to elucidate molecular structural variations that underlie these variations in CA assembly morphology. We find that multidimensional solid state NMR spectra of N-15, C-13-labeled CA assemblies are remarkably similar for the three morphologies, with only small differences in N-15 and C-13 chemical shifts, no significant differences in NMR line widths, and few differences in the number of detectable NMR cross-peaks. Thus, the pronounced differences in morphology do not involve major differences in the conformations and identities of structurally ordered protein segments. Instead, morphological variations are attributable to variations in conformational distributions within disordered segments, which do not contribute to the solid state NMR spectra. Variations in solid state NMR signals from certain amino acid side chains are also observed, suggesting differences in the intermolecular dimerization interface between curved and planar CA lattices, as well as possible differences in intramolecular helix-helix packing.
收录类别SCI ; EI
语种英语
资助项目NIDDK, National Institutes of Health[DK075032]
WOS研究方向Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
WOS记录号WOS:000379770500018
出版者AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI入藏号20162502527510
EI主题词Conformations ; Interface states ; Light polarization ; Morphology ; Nuclear magnetic resonance spectroscopy ; Proteins
EI分类号Light/Optics:741.1 ; Physical Chemistry:801.4 ; Organic Compounds:804.1 ; Classical Physics; Quantum Theory; Relativity:931 ; High Energy Physics; Nuclear Physics; Plasma Physics:932 ; Materials Science:951
WOS关键词HUMAN-IMMUNODEFICIENCY-VIRUS ; SOLID-STATE NMR ; NUCLEAR-MAGNETIC-RESONANCE ; ANGLE-SPINNING NMR ; CHEMICAL-SHIFTS ; GAG POLYPROTEIN ; TERMINAL DOMAIN ; DIMERIZATION DOMAIN ; CRYSTAL-STRUCTURE ; LATTICE FORMATION
原始文献类型Article
引用统计
文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1801
专题生命科学与技术学院_PI研究组_陆珺霞组
通讯作者Tycko, Robert
作者单位
1.NIDKK, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
2.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China
第一作者单位生命科学与技术学院
推荐引用方式
GB/T 7714
Lu, Jun-Xia,Bayro, Marvin J.,Tycko, Robert. Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(25):13098-13112.
APA Lu, Jun-Xia,Bayro, Marvin J.,&Tycko, Robert.(2016).Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.JOURNAL OF BIOLOGICAL CHEMISTRY,291(25),13098-13112.
MLA Lu, Jun-Xia,et al."Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments".JOURNAL OF BIOLOGICAL CHEMISTRY 291.25(2016):13098-13112.
条目包含的文件 下载所有文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
个性服务
查看访问统计
谷歌学术
谷歌学术中相似的文章
[Lu, Jun-Xia]的文章
[Bayro, Marvin J.]的文章
[Tycko, Robert]的文章
百度学术
百度学术中相似的文章
[Lu, Jun-Xia]的文章
[Bayro, Marvin J.]的文章
[Tycko, Robert]的文章
必应学术
必应学术中相似的文章
[Lu, Jun-Xia]的文章
[Bayro, Marvin J.]的文章
[Tycko, Robert]的文章
相关权益政策
暂无数据
收藏/分享
文件名: 10.1074@jbc.M116.720557.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。