CEEPC/IPM/CMSC - Abstrakt prezentace

(4. konference České společnosti pro hmotnostní spektrometrii - WeP-005)
Dynamics of chloride channel from E. coli studied by hydrogen/deuterium exchange.

Jiří Hausner 1,2 *, Merritt Maduke 3, Petr Novák 1,2, Petr Man 1,2, Daniel Kavan 1,2

  1. Institute of Microbiology, CAS, Prague, CZ
  2. Charles University in Prague, CZ
  3. Stanford University, Stanford, USA

Abstrakt

Chloride channels belong to an extensive family of transmembrane proteins, whose dysfunction causes a wide range of illnesses1. A detailed study of the structural changes during transport enables us to understand the transport mechanism and can provide valuable information required for effective treatment.

Considering the fact that mammalian chloride channels are usually produced with some difficulty, experiments are mainly done on bacterial alternatives which have shown to be quite similar to mammalian analogues. Till now the most explored representative is a bacterial chloride channel from E. coli (ClC-ec1), whose structure has been solved by X-ray crystallography 2. This technique as well as electrophysiological measurements have been so far the most widely used methods for studying of chloride channel transport mechanism.

Unlike these methods, hydrogen/deuterium exchange combined with mass spectrometry enables us to monitor dynamic conformation changes under different conditions directly in solution 3. Our research is focused on the study of structural changes of CLC-EC1 in dependence on protonation (pH 4.5 and 7.5) and the presence of different anions. These anions are more or less suitable substrates for this transporter and therefore help us to reveal the potential transport mechanism of CLC-EC1.

* Korespondující autor: hausner89@gmail.com

Literatura

  1. Chen T.: Annu. Rev. Physiol. 67, 809 (2005).
  2. Dutzler R., Campbell EB., Cadene M., Chait BT., MacKinnon R.,: Nature 300, 108 (2002).
  3. Engen JR., Anal. Chem. 81, 7870 (2009).

Poděkování:

The work was supported by the grant SVV–2015–389115.


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