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Chemical Compound Review

sulfanylsulfonylmethane     sulfanylsulfonylmethane

Synonyms:
 
 
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Disease relevance of sulfanylsulfonylmethane

 

High impact information on sulfanylsulfonylmethane

  • Mutants expressed robust K+ currents in Xenopus oocytes and reacted with methanethiosulfonate ethyltrimethylammonium in both closed and open conformations of the channel [6].
  • By comparing the rates of reaction of extracellularly and intracellularly added 2-aminoethyl methanethiosulfonate, we previously located the closed gate in the resting state between alphaG240 and alphaT244, in the predicted M1-M2 loop at the intracellular end of M2 [7].
  • The mutant protein Q457C was able to transport sugar, but transport was abolished after alkylation by methanethiosulfonate reagents [8].
  • Specifically, 2-[(5-fluoresceinyl)aminocarbonyl]ethyl methanethiosulfonate was conjugated to a free cysteine on loop C and to five substituted cysteines at strategic locations in the subunit sequence, and the backbone flexibility around each site of conjugation was measured with time-resolved fluorescence anisotropy [9].
  • At position 373, substitution of Arg or Cys also strongly accelerated desensitization: however, in the case of K373C the wild-type phenotype was fully restored by adding ethylammonium methanethiosulfonate [10].
 

Biological context of sulfanylsulfonylmethane

 

Anatomical context of sulfanylsulfonylmethane

 

Associations of sulfanylsulfonylmethane with other chemical compounds

  • Both cysteine residues were accessible from the periplasmic as well as from the cytoplasmic side of the membrane by the membrane-impermeable thiol reagent [2-(trimethylammonium)ethyl] methanethiosulfonate bromide (MTSET) suggesting that the residues are part of the translocation site [21].
  • Furthermore, the modification of Cys-423 with methyl methanethiosulfonate led to a shift of the allosteric transition toward the R-state, probably the result of increased hydrophobicity of the residue [22].
  • Pentobarbital activation of the receptor increased the rate of methanethiosulfonate modification of alpha(1)D62C and alpha(1)S68C, demonstrating that parts of the binding site undergo structural rearrangements during channel gating [23].
  • In D95C-containing receptors, application of MTS in the presence of SR95531 causes a greater effect on I(GABA) than MTS alone, suggesting that binding of a competitive antagonist can cause movements in the binding site [24].
  • These results, together with those from previous labeling studies with other thiol-reactive compounds, dibromobimane, MTS-verapamil, and MTS-cross-linker substrates, indicate that common residues are involved in the binding of structurally different drug substrates and that P-gp has a common drug-binding site [25].
 

Gene context of sulfanylsulfonylmethane

 

Analytical, diagnostic and therapeutic context of sulfanylsulfonylmethane

  • Residual fast inactivation of ICM-hH1a in fused tsA201 cells was abolished by intracellular perfusion with 2.5 mM 2-(trimethylammonium)ethyl methanethiosulfonate (MTSET) [31].
  • After treatment with palytoxin, six other positions (Y(778), L(780), S(782), P(785), E(786) and L(791)), distributed along the whole length of the segment, became readily accessible to a small-size methanethiosulfonate compound (2-aminoethyl methanethiosulfonate) [32].
  • The cancer-preventive properties of compounds and were tested in JB6 Cl41 mouse skin cells, using a variety of assessments, including the methanethiosulfonate (MTS) assay, flow cytometry, and soft agar assay [33].
  • The structural environment of the Q/R site and its positioning with regard to a narrow constriction were probed with the accessibility of substituted cysteines to positively and negatively charged methanethiosulfonate reagents, applied from the extracellular and cytoplasmic sides of the channel [34].
  • Apparently homogenous glycoproteins can be synthesised in good yield by a combination of site directed mutagenesis, a highly flexible but selective chemical derivatisation and efficient purification through the use of glycosyl thiosulfonates such as 2-((biotinoyl)-amino)-ethyl methanethiosulfonate [35].

References

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  18. Steroidal affinity labels of the estrogen receptor. 2. 17 alpha-[(Haloacetamido)alkyl]estradiols. el Garrouj, D., Aliau, S., Aumelas, A., Borgna, J.L. J. Med. Chem. (1995) [Pubmed]
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  21. Alternating access and a pore-loop structure in the Na+-citrate transporter CitS of Klebsiella pneumoniae. Sobczak, I., Lolkema, J.S. J. Biol. Chem. (2004) [Pubmed]
  22. Allosteric regulation of pyruvate kinase M2 isozyme involves a cysteine residue in the intersubunit contact. Ikeda, Y., Noguchi, T. J. Biol. Chem. (1998) [Pubmed]
  23. Different residues in the GABA(A) receptor alpha 1T60-alpha 1K70 region mediate GABA and SR-95531 actions. Holden, J.H., Czajkowski, C. J. Biol. Chem. (2002) [Pubmed]
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  26. Localization of a substrate binding domain of the human reduced folate carrier to transmembrane domain 11 by radioaffinity labeling and cysteine-substituted accessibility methods. Hou, Z., Stapels, S.E., Haska, C.L., Matherly, L.H. J. Biol. Chem. (2005) [Pubmed]
  27. Membrane topology of system xc- light subunit reveals a re-entrant loop with substrate-restricted accessibility. Gasol, E., Jiménez-Vidal, M., Chillarón, J., Zorzano, A., Palacín, M. J. Biol. Chem. (2004) [Pubmed]
  28. Chemical modification of the RTEM-1 thiol beta-lactamase by thiol-selective reagents: evidence for activation of the primary nucleophile of the beta-lactamase active site by adjacent functional groups. Knap, A.K., Pratt, R.F. Proteins (1989) [Pubmed]
  29. State-dependent chemical reactivity of an engineered cysteine reveals conformational changes in the outer vestibule of the cystic fibrosis transmembrane conductance regulator. Zhang, Z.R., Song, B., McCarty, N.A. J. Biol. Chem. (2005) [Pubmed]
  30. A role for the middle C terminus of G-protein-activated inward rectifier potassium channels in regulating gating. Guo, Y., Waldron, G.J., Murrell-Lagnado, R. J. Biol. Chem. (2002) [Pubmed]
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  32. Structure of the 5th transmembrane segment of the Na,K-ATPase alpha subunit: a cysteine-scanning mutagenesis study. Guennoun, S., Horisberger, J.D. FEBS Lett. (2000) [Pubmed]
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  34. Channel-lining residues of the AMPA receptor M2 segment: structural environment of the Q/R site and identification of the selectivity filter. Kuner, T., Beck, C., Sakmann, B., Seeburg, P.H. J. Neurosci. (2001) [Pubmed]
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