Rational Design, Binding Studies, and Crystal-Structure Evaluation of the First Ligand Targeting the Dimerization Interface of the 14-3-3ζ Adapter Protein

ChemBioChem ◽  
2018 ◽  
Vol 19 (6) ◽  
pp. 591-595 ◽  
Author(s):  
Martin Ehlers ◽  
Jean-Noël Grad ◽  
Sumit Mittal ◽  
David Bier ◽  
Marcel Mertel ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Rational Design ◽  
Adapter Protein ◽  
Binding Studies ◽  
Dimerization Interface ◽  
Structure Evaluation

Rational design and crystal structure prediction of ring-fused double-PDI compounds as n-channel organic semiconductors: a DFT study

2021 ◽  
Author(s):  
Suryakanti Debata ◽  
Smruti R. Sahoo ◽  
Rudranarayan Khatua ◽  
Sridhar Sahu
Keyword(s):  
Crystal Structure ◽  
Charge Transport ◽  
Organic Semiconductors ◽  
Structure Prediction ◽  
Rational Design ◽  
Molecular Design ◽  
Design Strategy ◽  
Dft Study ◽  
Crystal Structure Prediction ◽  
Model Compounds

In this study, we present an effective molecular design strategy to develop the n-type charge transport characteristics in organic semiconductors, using ring-fused double perylene diimides (DPDIs) as the model compounds.

scholarly journals Structure of the N-terminal dimerization domain of CEACAM7

2015 ◽  
Vol 71 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Daniel A. Bonsor ◽  
Dorothy Beckett ◽  
Eric J. Sundberg
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bond ◽  
Sequence Variation ◽  
Cellular Adhesion ◽  
Sedimentation Equilibrium ◽  
Colorectal Cancers ◽  
Dimerization Domain ◽  
Adhesion Protein ◽  
Dimerization Interface ◽  
Colon And Rectum

CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes theC′′ strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. TheKdimerizationfor CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulatedviasequence variation in the dimerization surface.

scholarly journals Structural analysis of point mutations at theVaccinia virusA20/D4 interface

2016 ◽  
Vol 72 (9) ◽  
pp. 687-691 ◽  
Author(s):  
Céline Contesto-Richefeu ◽  
Nicolas Tarbouriech ◽  
Xavier Brazzolotto ◽  
Wim P. Burmeister ◽  
Christophe N. Peyrefitte ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Structural Analysis ◽  
Complex Formation ◽  
Dna Polymerase ◽  
Point Mutations ◽  
Conformational Space ◽  
Uracil Dna Glycosylase ◽  
Dimerization Interface ◽  
Solvation Parameters

TheVaccinia viruspolymerase holoenzyme is composed of three subunits: E9, the catalytic DNA polymerase subunit; D4, a uracil-DNA glycosylase; and A20, a protein with no known enzymatic activity. The D4/A20 heterodimer is the DNA polymerase cofactor, the function of which is essential for processive DNA synthesis. The recent crystal structure of D4 bound to the first 50 amino acids of A20 (D4/A201–50) revealed the importance of three residues, forming a cation–π interaction at the dimerization interface, for complex formation. These are Arg167 and Pro173 of D4 and Trp43 of A20. Here, the crystal structures of the three mutants D4-R167A/A201–50, D4-P173G/A201–50and D4/A201–50-W43A are presented. The D4/A20 interface of the three structures has been analysed for atomic solvation parameters and cation–π interactions. This study confirms previous biochemical data and also points out the importance for stability of the restrained conformational space of Pro173. Moreover, these new structures will be useful for the design and rational improvement of known molecules targeting the D4/A20 interface.

scholarly journals Crystal structure of the M5muscarinic acetylcholine receptor

2019 ◽  
Vol 116 (51) ◽  
pp. 26001-26007 ◽  
Author(s):  
Ziva Vuckovic ◽  
Patrick R. Gentry ◽  
Alice E. Berizzi ◽  
Kunio Hirata ◽  
Swapna Varghese ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Acetylcholine Receptor ◽  
Rational Design ◽  
Structural Information ◽  
Family Members ◽  
Muscarinic Acetylcholine Receptor ◽  
Receptor Subtype ◽  
Ligand Interaction ◽  
Related Family ◽  
Allosteric Sites

The human M5muscarinic acetylcholine receptor (mAChR) has recently emerged as an exciting therapeutic target for treating a range of disorders, including drug addiction. However, a lack of structural information for this receptor subtype has limited further drug development and validation. Here we report a high-resolution crystal structure of the human M5mAChR bound to the clinically used inverse agonist, tiotropium. This structure allowed for a comparison across all 5 mAChR family members that revealed important differences in both orthosteric and allosteric sites that could inform the rational design of selective ligands. These structural studies, together with chimeric swaps between the extracellular regions of the M2and M5mAChRs, provided structural insight into kinetic selectivity, where ligands show differential residency times between related family members. Collectively, our study provides important insights into the nature of orthosteric and allosteric ligand interaction across the mAChR family that could be exploited for the design of selective drugs.

Synthesis, characterization, crystal structure and DNA, HSA-binding studies of four Schiff base complexes derived from salicylaldehyde and isopropylamine

2017 ◽  
Vol 466 ◽  
pp. 48-60 ◽  
Author(s):  
Monireh Dehkhodaei ◽  
Mahsa Khorshidifard ◽  
Hadi Amiri Rudbari ◽  
Mehdi Sahihi ◽  
Gholamhassan Azimi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Schiff Base ◽  
Schiff Base Complexes ◽  
Binding Studies

Crystal structure of nickel manganese-layered double hydroxide@cobaltosic oxides on nickel foam towards high-performance supercapacitors

CrystEngComm ◽  
2019 ◽  
Vol 21 (3) ◽  
pp. 470-477 ◽  
Author(s):  
Huihua Peng ◽  
Chuan Jing ◽  
Jie Chen ◽  
Deyi Jiang ◽  
Xiaoying Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Crystal Structures ◽  
Layered Double Hydroxide ◽  
High Performance ◽  
Rational Design ◽  
Electrode Materials ◽  
Nickel Foam ◽  
Double Hydroxide ◽  
Nickel Manganese

Rational design of the crystal structures of electrode materials is considered as an important strategy to construct high-performance supercapacitors.

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