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J Biol Chem, Vol. 275, Issue 18, 13683-13689, May 5, 2000
From the Department of Molecular Genetics and Biochemistry and the
Members of the heteropentameric ligand-gated ion
channel superfamily rapidly mediate signaling across the synaptic
cleft. Sequence analysis and limited experimental studies have yielded a topological model containing four transmembrane
Coupled Proteolytic and Mass Spectrometry Studies Indicate a
Novel Topology for the Glycine Receptor*
, and Department of Pathology, University of Pittsburgh
School of Medicine, Pittsburgh, Pennsylvania 15219
-helices, labeled M1 to M4, and a large soluble, extracellular N-terminal domain. This
model persists to date despite some recent structural studies that
suggest it may be inappropriate. In this study, the topology of the
glycine receptor was probed by limited proteolysis coupled to mass
spectrometry. Of particular note, accessible cleavage sites within the
putative M1 and M3 transmembrane helices were identified.
Membrane-associated fragments within the postulated globular
extracellular N-terminal domain were also observed. This report
presents several key details incorporated in a new topological model
and is the first direct experimental evidence that a subset of the
transmembrane regions are too short to be membrane-spanning -helices; rather, these regions are proposed to be a mix of
-helices and 
-sheets. This report is also the first to exploit
the capability of mass spectrometry to probe critically the topology of
a class of membrane proteins of unknown structure.
*
This work was supported by National Institutes of Health
Grant GM51911-01 (to M. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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