β-Amyrin synthase from Euphorbia tirucalli L. functional analyses of the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation–π and CH–π interactions for the efficient catalytic action of the polyolefin cyclization cascade

2017 ◽  
Vol 15 (1) ◽  
pp. 177-188 ◽  
Author(s):  
Ryousuke Ito ◽  
Chika Nakada ◽  
Tsutomu Hoshino
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Catalytic Action ◽  
Aromatic Residues ◽  
Π Interactions ◽  
Euphorbia Tirucalli ◽  
Functional Analyses

Investigation of functions of aromatic amino acids: steric bulk, cation–π and CH–π interactions.

scholarly journals Correction: β-Amyrin synthase from Euphorbia tirucalli L. functional analyses of the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation–π and CH–π interactions for the efficient catalytic action of the polyolefin cyclization cascade

2017 ◽  
Vol 15 (3) ◽  
pp. 717-717 ◽  
Author(s):  
Ryousuke Ito ◽  
Chika Nakada ◽  
Tsutomu Hoshino
Keyword(s):  
Catalytic Action ◽  
Aromatic Residues ◽  
Π Interactions ◽  
Euphorbia Tirucalli ◽  
Functional Analyses

Correction for ‘β-Amyrin synthase from Euphorbia tirucalli L. functional analyses of the highly conserved aromatic residues Phe413, Tyr259 and Trp257 disclose the importance of the appropriate steric bulk, and cation–π and CH–π interactions for the efficient catalytic action of the polyolefin cyclization cascade’ by Ryousuke Ito et al., Org. Biomol. Chem., 2017, 15, 177–188.

On the interaction between the imidazolium cation and aromatic amino acids. A computational study

2015 ◽  
Vol 13 (29) ◽  
pp. 7961-7972 ◽  
Author(s):  
Ana A. Rodríguez-Sanz ◽  
Enrique M. Cabaleiro-Lago ◽  
Jesús Rodríguez-Otero
Keyword(s):  
Amino Acids ◽  
Computational Study ◽  
Aromatic Amino Acids ◽  
Imidazolium Cation ◽  
Π Interactions

Phe, Tyr and Trp form parallel complexes with cation⋯π interactions. His complexes are the strongest, but without making contact with the aromatic cloud.

Serine and Cysteine π-Interactions in Nature: A Comparison of the Frequency, Structure, and Stability of Contacts Involving Oxygen and Sulfur

2015 ◽  
Vol 68 (3) ◽  
pp. 385 ◽  
Author(s):  
Hanzala B. Hussain ◽  
Katie A. Wilson ◽  
Stacey D. Wetmore
Keyword(s):  
Amino Acids ◽  
High Resolution ◽  
Protein Stability ◽  
Crystal Structures ◽  
Protein Complexes ◽  
Aromatic Amino Acids ◽  
Biological Macromolecules ◽  
Great Stability ◽  
Π Interactions ◽  
And Function

Despite many DNA–protein π-interactions in high-resolution crystal structures, only four X–H···π or X···π interactions were found between serine (Ser) or cysteine (Cys) and DNA nucleobase π-systems in over 100 DNA–protein complexes (where X = O for Ser and X = S for Cys). Nevertheless, 126 non-covalent contacts occur between Ser or Cys and the aromatic amino acids in many binding arrangements within proteins. Furthermore, Ser and Cys protein–protein π-interactions occur with similar frequencies and strengths. Most importantly, due to the great stability that can be provided to biological macromolecules (up to –20 kJ mol–1 for neutral π-systems or –40 kJ mol–1 for cationic π-systems), Ser and Cys π-interactions should be considered when analyzing protein stability and function.

scholarly journals Cation-π Interactions Involving Aromatic Amino Acids

2007 ◽  
Vol 137 (6) ◽  
pp. 1504S-1508S ◽  
Author(s):  
Dennis A. Dougherty
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Π Interactions

scholarly journals Aromatic Amino Acids in the Juxtamembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Are Important for Receptor-Dependent Virus Entry and Cell-Cell Fusion

2008 ◽  
Vol 82 (6) ◽  
pp. 2883-2894 ◽  
Author(s):  
Megan W. Howard ◽  
Emily A. Travanty ◽  
Scott A. Jeffers ◽  
M. K. Smith ◽  
Sonia T. Wennier ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Fusion ◽  
Transmembrane Domain ◽  
Virus Entry ◽  
Aromatic Amino Acids ◽  
Wild Type ◽  
Aromatic Residues ◽  
Wild Type Level ◽  
S Proteins ◽  
Cell Cell

ABSTRACT The severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein (S) is a class I viral fusion protein that binds to its receptor glycoprotein, human angiotensin converting enzyme 2 (hACE2), and mediates virus entry and cell-cell fusion. The juxtamembrane domain (JMD) of S is an aromatic amino acid-rich region proximal to the transmembrane domain that is highly conserved in all coronaviruses. Alanine substitutions for one or two of the six aromatic residues in the JMD did not alter the surface expression of the SARS-CoV S proteins with a deletion of the C-terminal 19 amino acids (S Δ19) or reduce binding to soluble human ACE2 (hACE2). However, hACE2-dependent entry of trypsin-treated retrovirus pseudotyped viruses expressing JMD mutant S Δ19 proteins was greatly reduced. Single alanine substitutions for aromatic residues reduced entry to 10 to 60% of the wild-type level. The greatest reduction was caused by residues nearest the transmembrane domain. Four double alanine substitutions reduced entry to 5 to 10% of the wild-type level. Rapid hACE2-dependent S-mediated cell-cell fusion was reduced to 60 to 70% of the wild-type level for all single alanine substitutions and the Y1188A/Y1191A protein. S Δ19 proteins with other double alanine substitutions reduced cell-cell fusion further, from 40% to less than 20% of wild-type levels. The aromatic amino acids in the JMD of the SARS-CoV S glycoprotein play critical roles in receptor-dependent virus-cell and cell-cell fusion. Because the JMD is so highly conserved in all coronavirus S proteins, it is a potential target for development of drugs that may inhibit virus entry and/or cell-cell fusion mediated by S proteins of all coronaviruses.

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