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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 | |
| Source Publication | JOURNAL OF BIOLOGICAL CHEMISTRY
 |
| ISSN | 0021-9258 |
| Volume | 291Issue:25Pages:13098-13112 |
| Status | 已发表 |
| DOI | 10.1074/jbc.M116.720557 |
| Abstract | 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. |
| Indexed By | SCI ; EI |
| Language | 英语 |
| Funding Project | NIDDK, National Institutes of Health[DK075032] |
| WOS Research Area | Biochemistry & Molecular Biology |
| WOS Subject | Biochemistry & Molecular Biology |
| WOS ID | WOS:000379770500018 |
| Publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| EI Accession Number | 20162502527510 |
| EI Keywords | Conformations ; Interface states ; Light polarization ; Morphology ; Nuclear magnetic resonance spectroscopy ; Proteins |
| EI Classification Number | 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 Keyword | HUMAN-IMMUNODEFICIENCY-VIRUS ; SOLID-STATE NMR ; NUCLEAR-MAGNETIC-RESONANCE ; ANGLE-SPINNING NMR ; CHEMICAL-SHIFTS ; GAG POLYPROTEIN ; TERMINAL DOMAIN ; DIMERIZATION DOMAIN ; CRYSTAL-STRUCTURE ; LATTICE FORMATION |
| Original Document Type | Article |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1801 |
| Collection | 生命科学与技术学院_PI研究组_陆珺霞组 |
| Corresponding Author | Tycko, Robert |
| Affiliation | 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 |
| First Author Affilication | School of Life Science and Technology |
| Recommended Citation 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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