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- W2612758524 abstract "Abstract Investigating the effect of pressure sheds light on the dynamics and plasticity of proteins, intrinsically correlated to functional efficiency. Here we detail the structural response to pressure of neuroglobin (Ngb), a hexacoordinate globin likely to be involved in neuroprotection. In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the “heme sliding mechanism”. Combining high pressure crystallography and coarse-grain simulations on wild type Ngb as well as two mutants, one (V101F) with unaffected and another (F106W) with decreased affinity for CO, we show that Ngb hinges around a rigid mechanical nucleus of five hydrophobic residues (V68, I72, V109, L113, Y137) during its conformational transition induced by gaseous ligand, that the intrinsic flexibility of the F-G loop appears essential to drive the heme sliding mechanism, and that residue Val 101 may act as a sensor of the interaction disruption between the heme and the distal histidine." @default.
- W2612758524 created "2017-05-19" @default.
- W2612758524 creator A5001379201 @default.
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- W2612758524 date "2017-05-12" @default.
- W2612758524 modified "2023-10-18" @default.
- W2612758524 title "Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography" @default.
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- W2612758524 doi "https://doi.org/10.1038/s41598-017-02097-1" @default.
- W2612758524 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5431840" @default.
- W2612758524 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28500341" @default.
- W2612758524 hasPublicationYear "2017" @default.
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