Article
Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states.
Acta crystallographica. Section D, Biological crystallography - 1 Oct 2013
Sander Bodo, Tria Giancarlo, Shkumatov Alexander V, Kim Eun-Young, Grossmann J Günter, Tessmer Ingrid, Svergun Dmitri I, Schindelin Hermann
Abstract excerpt
Gephyrin is a trimeric protein involved in the final steps of molybdenum-cofactor (Moco) biosynthesis and in the clustering of inhibitory glycine and GABAA receptors at postsynaptic specializations. Each protomer consists of stably folded domains (referred to as the G and E domains) located at either terminus and connected by a proteolytically sensitive linker of ∼150 residues. Both terminal domains can...
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