Diversity of Interactions in Redox Systems: From Short- to Long-Lived Complexes

Díaz‐Quintana, Antonio; Cruz-Gallardo, Isabel; Rosa, Miguel De La; Dı́az-Moreno, Irene

doi:10.1201/b19087-3

Cited by 1 publication

(3 citation statements)

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“…2,000 Å [ 16 ], in the verge between stable and transitory complexes [ 17 ]. This may provide the ability of modulating the lifetime of the complex by means of specific interactions [ 18 ]. Due to its long interaction range, electrostatics can be unspecific and lead to highly dynamic complexes [ 18 – 20 ].…”

Section: Introductionmentioning

confidence: 99%

“…This may provide the ability of modulating the lifetime of the complex by means of specific interactions [ 18 ]. Due to its long interaction range, electrostatics can be unspecific and lead to highly dynamic complexes [ 18 – 20 ]. However, residues with opposite charges at the rim of the binding interface may form salt-bridges, thereby stabilizing the complex and restraining its conformation dynamics [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

“…Due to its long interaction range, electrostatics can be unspecific and lead to highly dynamic complexes [ 18 – 20 ]. However, residues with opposite charges at the rim of the binding interface may form salt-bridges, thereby stabilizing the complex and restraining its conformation dynamics [ 18 ]. For instance, mutations of charged residues that break single salt bridges impair Ferredoxin binding to both Nitrite Reductase and Glutamate Synthase [ 21 ].…”

Section: Introductionmentioning

confidence: 99%

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The Dynamics of the Human Leukocyte Antigen Head Domain Modulates Its Recognition by the T-Cell Receptor

et al. 2016

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Generating the immune response requires the discrimination of peptides presented by the human leukocyte antigen complex (HLA) through the T-cell receptor (TCR). However, how a single amino acid substitution in the antigen bonded to HLA affects the response of T cells remains uncertain. Hence, we used molecular dynamics computations to analyze the molecular interactions between peptides, HLA and TCR. We compared immunologically reactive complexes with non-reactive and weakly reactive complexes. MD trajectories were produced to simulate the behavior of isolated components of the various p-HLA-TCR complexes. Analysis of the fluctuations showed that p-HLA binding barely restrains TCR motions, and mainly affects the CDR3 loops. Conversely, inactive p-HLA complexes displayed significant drop in their dynamics when compared with its free versus ternary forms (p-HLA-TCR). In agreement, the free non-reactive p-HLA complexes showed a lower amount of salt bridges than the responsive ones. This resulted in differences between the electrostatic potentials of reactive and inactive p-HLA species and larger vibrational entropies in non-elicitor complexes. Analysis of the ternary p-HLA-TCR complexes also revealed a larger number of salt bridges in the responsive complexes. To summarize, our computations indicate that the affinity of each p-HLA complex towards TCR is intimately linked to both, the dynamics of its free species and its ability to form specific intermolecular salt-bridges in the ternary complexes. Of outstanding interest is the emerging concept of antigen reactivity involving its interplay with the HLA head sidechain dynamics by rearranging its salt-bridges.

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