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MD Simulation Reveals Regulation of Mechanical Force and Extracellular Domain 2 on Binding of DNAM-1 to CD155.
Fang, Liping; Zhao, Yang; Guo, Pei; Fang, Ying; Wu, Jianhua.
Afiliação
  • Fang L; Institute of Biomechanics, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, China.
  • Zhao Y; Institute of Biomechanics, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, China.
  • Guo P; Institute of Biomechanics, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, China.
  • Fang Y; Institute of Biomechanics, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, China.
  • Wu J; Institute of Biomechanics, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, China.
Molecules ; 28(6)2023 Mar 21.
Article em En | MEDLINE | ID: mdl-36985819
Two extracellular domains of the adhesive receptor DNAM-1 are involved in various cellular biological processes through binding to ligand CD155, usually under a mechano-microenvironment. The first extracellular domain (D1) plays a key role in recognition, but the function of the second extracellular domain (D2) and effects of force on the interaction of DNAM-1 with CD155 remain unclear. We herein studied the interaction of DNAM-1 with CD155 by performing steered molecular dynamics (MD) simulations, and observed the roles of tensile force and D2 on the affinity of DNAM-1 to CD155. The results showed that D2 improved DNAM-1 affinity to CD155; the DNAM-1/CD155 complex had a high mechanical strength and a better mechanical stability for its conformational conservation either at pulling with constant velocity or under constant tensile force (≤100 pN); the catch-slip bond transition governed CD155 dissociation from DNAM-1; and, together with the newly assigned key residues in the binding site, force-induced conformation changes should be responsible for the mechanical regulation of DNAM-1's affinity to CD155. This work provided a novel insight in understanding the mechanical regulation mechanism and D2 function in the interaction of DNAM-1 with CD155, as well as their molecular basis, relevant transmembrane signaling, and cellular immune responses under a mechano-microenvironment.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Simulação de Dinâmica Molecular / Imunidade Celular Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Simulação de Dinâmica Molecular / Imunidade Celular Idioma: En Ano de publicação: 2023 Tipo de documento: Article