Faculty Opinions recommendation of NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment.

Author(s):  
Gottfried Otting
2016 ◽  
Vol 138 (13) ◽  
pp. 4393-4400 ◽  
Author(s):  
Julien Orts ◽  
Marielle Aulikki Wälti ◽  
May Marsh ◽  
Laura Vera ◽  
Alvar D. Gossert ◽  
...  

2012 ◽  
Vol 20 (2) ◽  
pp. 218-230
Author(s):  
Junfeng Huang ◽  
Riqiang Deng ◽  
Jinwen Wang ◽  
Hongkai Wu ◽  
Yuanyan Xiong ◽  
...  

2012 ◽  
Vol 180 (2) ◽  
pp. 318-326 ◽  
Author(s):  
Ke Wang ◽  
Korrinn Strunk ◽  
Gongpu Zhao ◽  
Jennifer L. Gray ◽  
Peijun Zhang

Methods ◽  
2018 ◽  
Vol 138-139 ◽  
pp. 26-38 ◽  
Author(s):  
Antoine Loquet ◽  
Nadia El Mammeri ◽  
Jan Stanek ◽  
Mélanie Berbon ◽  
Benjamin Bardiaux ◽  
...  

Genes ◽  
2018 ◽  
Vol 9 (9) ◽  
pp. 432 ◽  
Author(s):  
Chandran Nithin ◽  
Pritha Ghosh ◽  
Janusz Bujnicki

RNA-protein (RNP) interactions play essential roles in many biological processes, such as regulation of co-transcriptional and post-transcriptional gene expression, RNA splicing, transport, storage and stabilization, as well as protein synthesis. An increasing number of RNP structures would aid in a better understanding of these processes. However, due to the technical difficulties associated with experimental determination of macromolecular structures by high-resolution methods, studies on RNP recognition and complex formation present significant challenges. As an alternative, computational prediction of RNP interactions can be carried out. Structural models obtained by theoretical predictive methods are, in general, less reliable compared to models based on experimental measurements but they can be sufficiently accurate to be used as a basis for to formulating functional hypotheses. In this article, we present an overview of computational methods for 3D structure prediction of RNP complexes. We discuss currently available methods for macromolecular docking and for scoring 3D structural models of RNP complexes in particular. Additionally, we also review benchmarks that have been developed to assess the accuracy of these methods.


2021 ◽  
Author(s):  
Laia Miret Casals ◽  
Willem Vannecke ◽  
Kurt Hoogewijs ◽  
Gianluca Arauz ◽  
Marina Gay ◽  
...  

We describe furan as a triggerable ‘warhead’ for site-specific cross-linking using the actin and thymosin β4 (Tβ4)-complex as model of a weak and dynamic protein-protein interaction with known 3D structure...


2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Dieter Blaas

Abstract Rhinoviruses cause the common cold. They are icosahedral, built from sixty copies each of the capsid proteins VP1 through VP4 arranged in a pseudo T = 3 lattice. This shell encases a ss(+) RNA genome. Three-D classification of single and oligomeric asymmetric units computationally excised from a 2.9 Å cryo-EM density map of rhinovirus A89, showed that VP4 and the N-terminal extension of VP1 adopt different conformations within the otherwise identical 3D-structures. Analysis of up to sixty classes of single subunits and of six classes of subunit dimers, trimers, and pentamers revealed different orientations of the amino acid residues at the interface with the RNA suggesting that local asymmetry is dictated by disparities of the interacting nucleotide sequences. The different conformations escape detection by 3-D structure determination of entire virions with the conformational heterogeneity being only indicated by low density. My results do not exclude that the RNA follows a conserved assembly mechanism, contacting most or all asymmetric units in a specific way. However, as suggested by the gradual loss of asymmetry with increasing oligomerization and the 3D-structure of entire virions reconstructed by using Euler angles selected in the classification of single subunits, RNA path and/or folding likely differ from virion to virion.


Soft Matter ◽  
2014 ◽  
Vol 10 (47) ◽  
pp. 9446-9453 ◽  
Author(s):  
Oscar F. Aguilar Gutierrez ◽  
Alejandro D. Rey

We provide a proposed methodology for characterizing and reconstructing the 3D structure of biological plywoods from 2D experimental observations by considering the periodicity of the observed arcs and its intrinsic curvature, allowing the determination of p0 and h.


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