p(HBP:"VQIVYK motif")

Entity

Name

VQIVYK motif

Namespace

HBP

Namespace Version

20181119

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/90e1cb9e5e882703380c9db8d4915ac6f3cba137/export/hbp-names.belns

This result suggests that the VQIVYK peptide plays a role in the interaction between Hsp90 and tau protein, a hypothesis which is also supported by the fact that a tau variant deleted for the peptide VQIVYK was unable to interact with Hsp90 under immunoprecipitation conditions (Fig. 2B). PubMed:19363271

CA and the oxidized form of EC (ECox) inhibited tau aggregation in vitro due to their interaction with the two cysteine residues in tau. A synthetic peptide, SKCGS, representing the actual tau sequence, identified the thiol as reacting with CA and ECox which necessitates of cysteine for aggregation inhibition by CA. PubMed:23531502

We identified a novel molecular interaction implying the PHF6 peptide of Tau and the FK1/FK2 domains of FKBP52 independent of FK506 binding; suggesting a non-catalytic molecular interaction that might govern the effect of FKBP52 on Tau. PubMed:26903089

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

Two hexapeptide motifs at the beginning of R2 and R3 promote paired helical filament (PHF) aggregation by inducing β-structure. PubMed:17493042

This result suggests that the VQIVYK peptide plays a role in the interaction between Hsp90 and tau protein, a hypothesis which is also supported by the fact that a tau variant deleted for the peptide VQIVYK was unable to interact with Hsp90 under immunoprecipitation conditions (Fig. 2B). PubMed:19363271

This result suggests that the VQIVYK peptide plays a role in the interaction between Hsp90 and tau protein, a hypothesis which is also supported by the fact that a tau variant deleted for the peptide VQIVYK was unable to interact with Hsp90 under immunoprecipitation conditions (Fig. 2B). PubMed:19363271

CA and the oxidized form of EC (ECox) inhibited tau aggregation in vitro due to their interaction with the two cysteine residues in tau. A synthetic peptide, SKCGS, representing the actual tau sequence, identified the thiol as reacting with CA and ECox which necessitates of cysteine for aggregation inhibition by CA. PubMed:23531502

CA and the oxidized form of EC (ECox) inhibited tau aggregation in vitro due to their interaction with the two cysteine residues in tau. A synthetic peptide, SKCGS, representing the actual tau sequence, identified the thiol as reacting with CA and ECox which necessitates of cysteine for aggregation inhibition by CA. PubMed:23531502

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

We also show that two of the tau mutations found in hereditary frontotemporal dementias, DeltaK280 and P301L, have a much stronger tendency for PHF aggregation which correlates with their high propensity for beta-structure around the hexapeptide motifs. PubMed:11606569

We identified a novel molecular interaction implying the PHF6 peptide of Tau and the FK1/FK2 domains of FKBP52 independent of FK506 binding; suggesting a non-catalytic molecular interaction that might govern the effect of FKBP52 on Tau. PubMed:26903089

The two short hexapeptide motifs VQIINK and VQIVYK at the beginning of R2 and R3, respectively, show propensity for forming β‑sheet structures and are essential for tau aggregation, even though they comprise only a tiny fraction of the sequence PubMed:26631930

Disruption of these motifs (for example, by Pro mutations) abrogates the tendency for tau to aggregate; by contrast, strengthening the β‑structure with certain mutations (for instance, ΔK280 or P301L) accelerates tau aggregation both in vitro and in vivo PubMed:26631930

The motif VQIVYK has been shown to be sufficient to form fibrils composed of steric ‘zippers’ formed by two tightly interdigitated β‑sheets. PubMed:26631930