scholarly journals The Solution Structure of the AppA BLUF Domain: Insight into the Mechanism of Light-Induced Signaling

ChemBioChem ◽  
2005 ◽  
Vol 7 (1) ◽  
pp. 187-193 ◽  
Author(s):  
Jeffrey S. Grinstead ◽  
Shang-Te D. Hsu ◽  
Wouter Laan ◽  
Alexandre M. J. J. Bonvin ◽  
Klaas J. Hellingwerf ◽  
...  
Keyword(s):  
Solution Structure ◽  
Bluf Domain ◽  
Insight Into

scholarly journals Insight into the HIV-1 Vif SOCS-box–ElonginBC interaction

Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  
Keyword(s):  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Dynamic Information ◽  
Ubiquitin Ligase Complex ◽  
Biophysical Studies ◽  
Viral Infectivity Factor ◽  
Β Sheet ◽  
Socs Box ◽  
Insight Into ◽  
Hiv 1

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

scholarly journals Dilute Solution Structure of Bottlebrush Polymers

2019 ◽  
Author(s):  
Sarit Dutta ◽  
Matthew A. Wade ◽  
Dylan J. Walsh ◽  
Damien Guironnet ◽  
Simon A. Rogers ◽  
...  
Keyword(s):  
Brownian Dynamics ◽  
Solution Structure ◽  
Coarse Grained ◽  
Poly Lactic Acid ◽  
Linear Polymers ◽  
Molecular Architecture ◽  
Wide Range ◽  
Conformational Properties ◽  
Atomistic Structure ◽  
Insight Into

<div>Bottlebrush polymers are a class of macromolecules that has recently found use</div><div>in a wide variety of materials, ranging from lubricating brushes and</div><div>nanostructured coatings to elastomeric gels that exhibit structural color. These</div><div>polymers are characterized by dense branches extending from a central backbone,</div><div>and thus have properties distinct from linear polymers. It remains a challenge</div><div>to specifically understand conformational properties of these molecules, due to</div><div>the wide range of architectural parameters that can be present in a system, and</div><div>thus there is a need to accurately characterize and model these molecules. In</div><div>this paper, we use a combination of viscometry, light scattering, and computer</div><div>simulations to gain insight into the conformational properties of dilute</div><div>bottlebrush polymers. We focus on a series of model bottlebrushes consisting of</div><div>a poly(norbornene) (PNB) backbone with poly(lactic acid) (PLA) side chains. We</div><div>demonstrate that intrinsic viscosity and hydrodynamic radius are experimental</div><div>observations \emph{sensitive} to molecular architecture, exhibiting distinct</div><div>differences with different choices of branch and backbone lengths. Informed by</div><div>the atomistic structure of this PNB-PLA system, we rationalize a coarse-grained</div><div>simulation model that we evaluate using a combination of Brownian Dynamics and</div><div>Monte Carlo simulations. We show that this exhibits quantitative matching to</div><div>experimental results, enabling us to characterize the overall shape of the</div><div>bottlebrush via a number of metrics that can be extended to more general</div><div>bottlebrush architectures.</div>

scholarly journals Mechanistic Insight into Humanether-à-go-go-related Gene (hERG) K+Channel Deactivation Gating from the Solution Structure of the EAG Domain

2010 ◽  
Vol 286 (8) ◽  
pp. 6184-6191 ◽  
Author(s):  
Frederick W. Muskett ◽  
Samrat Thouta ◽  
Steven J. Thomson ◽  
Alexander Bowen ◽  
Phillip J. Stansfeld ◽  
...  
Keyword(s):  
Solution Structure ◽  
K Channel ◽  
Related Gene ◽  
Mechanistic Insight ◽  
Insight Into

Structure and Insight into Blue Light-Induced Changes in the BlrP1 BLUF Domain†,‡

Biochemistry ◽  
2009 ◽  
Vol 48 (12) ◽  
pp. 2620-2629 ◽  
Author(s):  
Qiong Wu ◽  
Kevin H. Gardner
Keyword(s):  
Blue Light ◽  
Bluf Domain ◽  
Induced Changes ◽  
Insight Into

Solution Structure of TT30, a Novel Complement Therapeutic Agent, Provides Insight into Its Joint Binding to Complement C3b and C3d

2012 ◽  
Vol 418 (3-4) ◽  
pp. 248-263 ◽  
Author(s):  
Keying Li ◽  
Jayesh Gor ◽  
V. Michael Holers ◽  
Michael J. Storek ◽  
Stephen J. Perkins
Keyword(s):  
Solution Structure ◽  
Therapeutic Agent ◽  
Insight Into

scholarly journals From Crystallographic Data to Solution Structure of Photoreceptors: The Case of AppA BLUF Domain

2021 ◽  
Author(s):  
Shaima Hashem ◽  
Veronica Macaluso ◽  
Michele Nottoli ◽  
Filippo Lipparini ◽  
Lorenzo Cupellini ◽  
...  
Keyword(s):  
Solution Structure ◽  
Molecular Mechanisms ◽  
Md Simulations ◽  
Hydrogen Bond Network ◽  
Light Activation ◽  
Activated State ◽  
Bond Network ◽  
Bluf Domain ◽  
First Time

<div>Photoreceptor proteins bind a chromophore, which, upon light absorption, modifies its geometry or its interactions with the protein, finally inducing the structural change needed to switch the protein from an inactive to an active or signaling state. In the Blue Light-Using Flavin (BLUF) family of photoreceptors, the chromophore is a flavin and the changes have been connected with a rearrangement of the hydrogen bond network around it on the basis of spectroscopic changes measured for the dark-to-light conversion. However, the exact conformational change triggered by the photoexcitation is still elusive mainly because a clear consensus on the identity not only of the light activated state but also of the dark one has not been achieved. Here, for the first time, we present an integrated investigation that combines microsecond MD simulations starting from the two conflicting crystal structures available for the AppA BLUF domain with calculations of NMR, IR and UV-Vis spectra using a polarizable QM/MM approach. Thanks to such a combined analysis of the three different spectroscopic responses, a robust characterization of the structure of the dark state in solution is given together with the uncovering of important flaws of the most popular molecular mechanisms present in the literature for the dark-to-light activation. </div>

scholarly journals NMR solution structure of tricyclo-DNA containing duplexes: insight into enhanced thermal stability and nuclease resistance

2019 ◽  
Vol 47 (9) ◽  
pp. 4872-4882 ◽  
Author(s):  
Andrei Istrate ◽  
Silke Johannsen ◽  
Alena Istrate ◽  
Roland K O Sigel ◽  
Christian J Leumann
Keyword(s):  
Thermal Stability ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Nuclease Resistance ◽  
Insight Into
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