Front Cover: Insights into the Structural and Energetic Descriptions of Ubiquitin Specific Protease 7

• Published in: ChemCatChem Vol. 15; no. 17
• Main Authors: José Luis Velázquez‐Libera, Caballero, Julio, Jans Alzate‐Morales, J Javier Ruiz‐Pernía, Tuñón, Iñaki
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley Subscription Services, Inc 01.09.2023
• Subjects: Construction industry; Histidine; Molecular dynamics; Reaction mechanisms; Rhodamine; Substrates
• ISSN: 1867-3880; 1867-3899
• DOI: 10.1002/cctc.202301008

The Front Cover, designed by Alex Pelayo, shows the active site of USP7, represented as the place where construction workers adjust the substrate (Ubiquitin‐Rhodamine 110, Ub‐Rho), so that it is in the ideal arrangement for the catalytic reaction to occur. Essential in this arrangement are the orientations of a cysteine (Cys223) and a histidine (His464) known as the catalytic dyad (represented at the left). An aspartate (Asp481, below left) and an asparagine (Asn218, at the top) are also involved. These residues fulfill roles that can be understood from molecular models and theoretical calculations. In their Research Article, J. L. Velázquez‐Libera, J. Caballero, I. Tuñón and co‐workers report the first computational study on the USP7 reaction mechanism with the substrate Ub‐Rho using a robust methodology that included molecular dynamics (MD) and hybrid QM/MM simulations with the adaptive string method (ASM). More information can be found in the Research Article by J. L. Velázquez‐Libera, J. Caballero, I. Tuñón and co‐workers.