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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 |
ISSN | 0021-9258 |
卷号 | 291期号:25页码:13098-13112 |
发表状态 | 已发表 |
DOI | 10.1074/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. |
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