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Dimethano-lbis[N'-(3-pyridylmethyl-ene)benzohydrazide]sodium(I) iodide.

ABSTRACT: The molecule of the title compound, [Na(C(13)H(11)N(3)O)(2)(CH(3)OH)(2)]I, is non-planar, with the Na atom chelated by the O atoms and the N atoms of two N'-(3-pyridylmethyl-ene)benzohydrazide ligands and both O atoms of two methanol ligands. The asymmetric unit consists of one half-mol-ecule. The Na atom is located on a crystallographic centre of inversion. The six-coordinate Na atom adopts a distorted octa-hedral coordination. In the crystal structure, inter-molecular N-H?I and O-H?N hydrogen bonds link the mol-ecules into a two-dimensional network.

SUBMITTER: Cui LS

PROVIDER: S-EPMC2967884 | biostudies-other | 2008

REPOSITORIES: biostudies-other

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Dimethano-lbis[N'-(3-pyridylmethyl-ene)benzohydrazide]sodium(I) iodide.

Cui Lian-Sheng LS Yin Han-Dong HD Yang Ming-Lei ML Wang Da-Qi DQ

Acta crystallographica. Section E, Structure reports online 20081210 Pt 1

The molecule of the title compound, [Na(C(13)H(11)N(3)O)(2)(CH(3)OH)(2)]I, is non-planar, with the Na atom chelated by the O atoms and the N atoms of two N'-(3-pyridylmethyl-ene)benzohydrazide ligands and both O atoms of two methanol ligands. The asymmetric unit consists of one half-mol-ecule. The Na atom is located on a crystallographic centre of inversion. The six-coordinate Na atom adopts a distorted octa-hedral coordination. In the crystal structure, inter-molecular N-H⋯I and O-H⋯N hydrogen ...[more]

PMID: 21581510

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Project description:Background: The ability of thyroid follicular epithelial cells to accumulate iodide via the sodium/iodide symporter (NIS) is exploited to successfully treat most thyroid cancers, although a subset of patients lose functional NIS activity and become unresponsive to radioiodide therapy, with poor clinical outcome. Our knowledge of NIS regulation remains limited, however. While numerous membrane proteins are functionally regulated via dimerization, there is little definitive evidence of NIS dimerization, and whether this might impact upon radioiodide uptake and treatment success is entirely unknown. We hypothesized that NIS dimerizes and that dimerization is a prerequisite for iodide uptake. Methods: Coimmunoprecipitation, proximity ligation, and Förster resonance energy transfer (FRET) assays were used to assess NIS:NIS interaction. To identify residues involved in dimerization, a homology model of NIS structure was built based on the crystal structure of the dimeric bacterial protein vSGLT. Results: Abundant cellular NIS dimerization was confirmed in vitro via three discrete methodologies. FRET and proximity ligation assays demonstrated that while NIS can exist as a dimer at the plasma membrane (PM), it is also apparent in other cellular compartments. Homology modeling revealed one key potential site of dimeric interaction, with six residues <3Å apart. In particular, NIS residues Y242, T243, and Q471 were identified as critical to dimerization. Individual mutation of residues Y242 and T243 rendered NIS nonfunctional, while abrogation of Q471 did not impact radioiodide uptake. FRET data show that the putative dimerization interface can tolerate the loss of one, but not two, of these three clustered residues. Conclusions: We show for the first time that NIS dimerizes in vitro, and we identify the key residues via which this happens. We hypothesize that dimerization of NIS is critical to its trafficking to the PM and may therefore represent a new mechanism that would need to be considered in overcoming therapeutic failure in patients with thyroid cancer.

Dataset Information

Dimethano-lbis[N'-(3-pyridylmethyl-ene)benzohydrazide]sodium(I) iodide.

Publications

Dimethano-lbis[N'-(3-pyridylmethyl-ene)benzohydrazide]sodium(I) iodide.

Similar Datasets

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