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Review
. 1999 Feb;113(2):163-70.
doi: 10.1085/jgp.113.2.163.

Ion channel assembly: creating structures that function

W N Green  1
Affiliations
Review

Ion channel assembly: creating structures that function

W N Green. J Gen Physiol. 1999 Feb.
No abstract available

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Figures

Figure 1
Figure 1
Consensus membrane topology of the AChR subunits. M1–M4 represent putative transmembrane regions.
Figure 2
Figure 2
The two models of AChR assembly. Subunit folding reactions are denoted by the filled arrows and oligomerization events by the open arrows. (A) Formation of the Bgt binding sites and the mAb 35 epitope precedes all subunit associations. The two different ACh binding sites, the high affinity dTC site (dTC) and the low affinity dTC site (ACh), appear on αγ or αδ heterodimers, respectively. (B) A conformational change in the α subunit cystine loop region and the formation of the first Bgt binding site and mAb 14 epitope occur on αβγ trimers. A conformational change in the β subunit cystine loop region and formation of the first ACh binding site, the high affinity dTC site, occur on αβγδ tetramers. Finally, the second Bgt and ACh binding sites appear on α2βγδ pentamers. Note that we are not proposing that subunits in the trimers and tetramers reposition to allow the insertion of unassembled δ and α subunits. This is only shown to illustrate the possible links between the subunit additions and the conformational changes on the trimers and tetramers.
See this image and copyright information in PMC

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