scholarly journals An insight into SARS-CoV-2 Membrane protein interaction with Spike, Envelope, and Nucleocapsid proteins

2020 ◽  
Author(s):  
Amit kumar ◽  
Prateek Kumar ◽  
Neha Garg ◽  
Rajanish Giri
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Protein Complex ◽  
Drug Targets ◽  
Virus Assembly ◽  
Protein Docking ◽  
Structural Proteins ◽  
Valuable Insight ◽  
Nucleocapsid Proteins ◽  
Insight Into

AbstractIntraviral protein-protein interactions are crucial for replication, pathogenicity, and viral assembly. Among these, virus assembly is a critical step as it regulates the arrangements of viral structural proteins and helps in the encapsulation of genomic material. SARS-CoV-2 structural proteins play an essential role in the self-rearrangement, RNA encapsulation, and mature virus particle formation. In SARS-CoV, the membrane protein interacts with the envelope and spike protein in Endoplasmic Reticulum Golgi Intermediate Complex (ERGIC) to form an assembly in the lipid bilayer, followed by membrane-ribonucleoprotein (nucleocapsid) interaction. In this study, using protein-protein docking, we tried to understand the interaction of membrane protein’s interaction with envelope, spike and nucleocapsid proteins. Further, simulation studies performed up to 100ns agreed that protein complexes M-E, M-S, and M-N were stable. Moreover, the calculated free binding energy and dissociation constant values support the protein complex formation. The interaction identified in the study will be of great importance, as it provides valuable insight into the protein complex, which could be the potential drug targets for future studies.

scholarly journals A 3D Model of the Membrane Protein Complex Formed by the White Spot Syndrome Virus Structural Proteins

PLoS ONE ◽  
2010 ◽  
Vol 5 (5) ◽  
pp. e10718 ◽  
Author(s):  
Yun-Shiang Chang ◽  
Wang-Jing Liu ◽  
Cheng-Chung Lee ◽  
Tsung-Lu Chou ◽  
Yuan-Ting Lee ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
3D Model ◽  
White Spot Syndrome Virus ◽  
White Spot ◽  
Structural Proteins ◽  
Membrane Protein Complex ◽  
White Spot Syndrome

scholarly journals Crystal Structure of the Epo1-Bem3 Complex for Bud Growth

2021 ◽  
Vol 22 (8) ◽  
pp. 3812
Author(s):  
Jin Wang ◽  
Lei Li ◽  
Zhenhua Ming ◽  
Lijie Wu ◽  
Liming Yan
Keyword(s):  
Crystal Structure ◽  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Protein Complex ◽  
Molecular Architecture ◽  
Hydrogen Deuterium ◽  
Bud Growth ◽  
Structural Insight ◽  
Guanosine Triphosphatase ◽  
Insight Into

Tubules of the endoplasmic reticulum (ER) spread into the buds of yeast by an actin-based mechanism and, upon entry, become attached to the polarisome, a proteinaceous micro-compartment below the tip of the bud. The minimal tether between polarisome and cortical ER is formed by a protein complex consisting of Epo1, a member of the polarisome, Scs2, a membrane protein of the ER and Cdc42 guanosine triphosphatase-activating protein Bem3. Here, we report the crystal structure of a complex between Epo1 and Bem3. In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1. Our findings provide a first structural insight into the molecular architecture of the link between cortical ER and the polarisome.

scholarly journals Mutations in the exocyst component EXOC2 cause severe defects in human brain development

2020 ◽  
Vol 217 (10) ◽  
Author(s):  
Nicole J. Van Bergen ◽  
Syed Mukhtar Ahmed ◽  
Felicity Collins ◽  
Mark Cowley ◽  
Annalisa Vetro ◽  
...  
Keyword(s):  
Motor Skills ◽  
Neural Development ◽  
Protein Complex ◽  
Valuable Insight ◽  
Neuronal Function ◽  
Nonsense Mediated Decay ◽  
Pathogenic Variants ◽  
Human Brain Development ◽  
Severe Reduction ◽  
Insight Into

The exocyst, an octameric protein complex, is an essential component of the membrane transport machinery required for tethering and fusion of vesicles at the plasma membrane. We report pathogenic variants in an exocyst subunit, EXOC2 (Sec5). Affected individuals have severe developmental delay, dysmorphism, and brain abnormalities; variability associated with epilepsy; and poor motor skills. Family 1 had two offspring with a homozygous truncating variant in EXOC2 that leads to nonsense-mediated decay of EXOC2 transcript, a severe reduction in exocytosis and vesicle fusion, and undetectable levels of EXOC2 protein. The patient from Family 2 had a milder clinical phenotype and reduced exocytosis. Cells from both patients showed defective Arl13b localization to the primary cilium. The discovery of mutations that partially disable exocyst function provides valuable insight into this essential protein complex in neural development. Since EXOC2 and other exocyst complex subunits are critical to neuronal function, our findings suggest that EXOC2 variants are the cause of the patients’ neurological disorders.

Study of the resistor material of an automotive spark plug by use of the charge-up effect along with elemental mapping in an electron microprobe

1991 ◽  
Vol 49 ◽  
pp. 742-743
Author(s):  
D. R. Liu ◽  
S. S. Shinozaki ◽  
J. S. Park ◽  
B. N. Juterbock
Keyword(s):  
Electron Microprobe ◽  
Present Report ◽  
Coated Sample ◽  
Valuable Insight ◽  
Elemental Mapping ◽  
Spark Plug ◽  
Carbon Coated ◽  
Electron Image ◽  
Electron Imaging ◽  
Insight Into

The electric and thermal properties of the resistor material in an automotive spark plug should be stable during its service lifetime. Containing many elements and many phases, this material has a very complex microstructure. Elemental mapping with an electron microprobe can reveal the distribution of all relevant elements throughout the sample. In this work, it is demonstrated that the charge-up effect, which would distort an electron image and, therefore, is normally to be avoided in an electron imaging work, could be used to advantage to reveal conductive and resistive zones in a sample. Its combination with elemental mapping can provide valuable insight into the underlying conductivity mechanism of the resistor.This work was performed in a CAMECA SX-50 microprobe. The spark plug used in the present report was a commercial product taken from the shelf. It was sectioned to expose the cross section of the resistor. The resistor was known not to contain the precious metal Au as checked on the carbon coated sample. The sample was then stripped of carbon coating and re-coated with Au.

Quantum Mechanical Interpretation of the Ultra-Low Energy Methyl-Rotation Dynamics in Porous Metal-Organic Frameworks Probed by Low-Frequency Vibrational Spectroscopy and ab initio Simulations

2018 ◽  
Author(s):  
Qi Li ◽  
Adam J. Zaczek ◽  
Timothy M. Korter ◽  
J. Axel Zeitler ◽  
Michael T. Ruggiero
Keyword(s):  
Ab Initio ◽  
Metal Organic Frameworks ◽  
Low Frequency ◽  
Rotor Dynamics ◽  
Quantum Mechanical ◽  
Valuable Insight ◽  
Void Space ◽  
Ab Initio Simulations ◽  
Metal Organic ◽  
Insight Into

<div>Understanding the nature of the interatomic interactions present within the pores of metal-organic frameworks</div><div>is critical in order to design and utilize advanced materials</div><div>with desirable applications. In ZIF-8 and its cobalt analogue</div><div>ZIF-67, the imidazolate methyl-groups, which point directly</div><div>into the void space, have been shown to freely rotate - even</div><div>down to cryogenic temperatures. Using a combination of ex-</div><div>perimental terahertz time-domain spectroscopy, low-frequency</div><div>Raman spectroscopy, and state-of-the-art ab initio simulations,</div><div>the methyl-rotor dynamics in ZIF-8 and ZIF-67 are fully charac-</div><div>terized within the context of a quantum-mechanical hindered-</div><div>rotor model. The results lend insight into the fundamental</div><div>origins of the experimentally observed methyl-rotor dynamics,</div><div>and provide valuable insight into the nature of the weak inter-</div><div>actions present within this important class of materials.</div>

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