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4BON

The structure and super-organization of acetylcholine receptor-rapsyn complexes class B

Summary for 4BON
Entry DOI10.2210/pdb4bon/pdb
Related4BOG 4BOI 4BOO
EMDB information2378
DescriptorACETYLCHOLINE RECEPTOR SUBUNIT ALPHA, ACETYLCHOLINE RECEPTOR BETA SUBUNIT, ACETYLCHOLINE RECEPTOR DELTA SUBUNIT, ... (4 entities in total)
Functional Keywordstransport protein, neurotransmitter receptor, clustering, synapse, neuromuscular junction, nicotinic, 43k
Biological sourceTORPEDO MARMORATA (MARBLED ELECTRIC RAY)
More
Cellular locationCell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P02711
Total number of polymer chains5
Total formula weight279950.34
Authors
Zuber, B.,Unwin, N. (deposition date: 2013-05-21, release date: 2013-06-26, Last modification date: 2024-10-09)
Primary citationZuber, B.,Unwin, N.
Structure and Superorganization of Acetylcholine Receptor-Rapsyn Complexes.
Proc.Natl.Acad.Sci.USA, 110:10622-, 2013
Cited by
PubMed Abstract: The scaffolding protein at the neuromuscular junction, rapsyn, enables clustering of nicotinic acetylcholine receptors in high concentration and is critical for muscle function. Patients with insufficient receptor clustering suffer from muscle weakness. However, the detailed organization of the receptor-rapsyn network is poorly understood: it is unclear whether rapsyn first forms a wide meshwork to which receptors can subsequently dock or whether it only forms short bridges linking receptors together to make a large cluster. Furthermore, the number of rapsyn-binding sites per receptor (a heteropentamer) has been controversial. Here, we show by cryoelectron tomography and subtomogram averaging of Torpedo postsynaptic membrane that receptors are connected by up to three rapsyn bridges, the minimum number required to form a 2D network. Half of the receptors belong to rapsyn-connected groups comprising between two and fourteen receptors. Our results provide a structural basis for explaining the stability and low diffusion of receptors within clusters.
PubMed: 23754381
DOI: 10.1073/PNAS.1301277110
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (40 Å)
Structure validation

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