Planar molecular arrangements aid the design of MHC class II binding peptides

Cortés, Adrián; Coral, Jonathan; McLachlan, C.; Benítez, Ricardo; Pinilla, Laura

doi:10.1134/s002689331702008x

Cited by 1 publication

(3 citation statements)

References 33 publications

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“…All these residues showed planar spatial patterns, as seen in Figure 1 where the electrical peptide-recognition residues D28 and E94 of the TCR are observed to act as couplings for the positive charges of the coupled peptide. This type of plane was also found in HLA-II molecules, as we have previously indicated (Cortés et al, 2013, Cortés et al, 2017b.…”

Section: Tcr Activation Mechanism According To the Tm-pecc-i Modelsupporting

confidence: 84%

“…In earlier work, we observed that planar molecular patterns were present in Major Complex Histocompatibility Class II (MHC-II) molecules. The patterns, known as Planar Electromagnetic fields of Cortés-Coral (or PECC), enabled us to present a coherent explanation of the process of MHC-II coupling with foreign peptides (Cortés et al, 2017b;Cortés et al, 2017a). PECC are also found in other proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Gly) arranged on the same plane within the protein, extending across the macromolecule. The result is the organized presence, in the internal protein structure, of specific PECC-Gly planes, PECC-Pro planes, PECC-Leu planes, and so on (Cortés et al, 2013;Cortes and Coral, 2015;Cortés et al, 2017b). Importantly, from crystal structure analysis of the planes, using Molecular Viewer software, and studying the behavior of the fully conserved residues it is possible to infer that all the component residues are mutually interlinked by a single electromagnetic field, which shows the same planar geometric form in all of the molecules studied.…”

Section: Introductionmentioning

confidence: 99%

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Molecular transduction in receptor-ligand systems by planar electromagnetic fields

Cortés¹,

Coral²,

McLachlan³

et al. 2022

Braz. J. Biol.

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The coupling of a ligand with a molecular receptor induces a signal that travels through the receptor, reaching the internal domain and triggering a response cascade. In previous work on T-cell receptors and their coupling with foreign antigens, we observed the presence of planar molecular patterns able to generate electromagnetic fields within the proteins. These planes showed a coherent (synchronized) behavior, replicating immediately in the intracellular domain that which occurred in the extracellular domain as the ligand was coupled. In the present study, we examined this molecular transduction - the capacity of the coupling signal to penetrate deep inside the receptor molecule and induce a response. We verified the presence of synchronized behavior in diverse receptor-ligand systems. To appreciate this diversity, we present four biochemically different systems - TCR-peptide, calcium pump-ADP, haemoglobin-oxygen, and gp120-CD4 viral coupling. The confirmation of synchronized molecular transduction in each of these systems suggests that the proposed mechanism would occur in all biochemical receptor-ligand systems.

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Section: Tcr Activation Mechanism According To the Tm-pecc-i Modelsupporting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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