4BOG
The structure and super-organization of acetylcholine receptor-rapsyn complexes
Summary for 4BOG
| Entry DOI | 10.2210/pdb4bog/pdb |
| Related | 4BOI 4BON 4BOO 4BOR 4BOT |
| EMDB information | 2376 |
| Descriptor | Acetylcholine receptor beta subunit, Acetylcholine receptor delta subunit, Acetylcholine receptor subunit alpha, ... (4 entities in total) |
| Functional Keywords | transport protein, clustering, synapse, neuromuscular junction, nicotinic, rapsyn, 43k, electric organ |
| Biological source | Torpedo marmorata (Marbled electric ray) More |
| Total number of polymer chains | 30 |
| Total formula weight | 1679702.02 |
| Authors | |
| Primary citation | Zuber, 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: 23754381DOI: 10.1073/PNAS.1301277110 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (50 Å) |
Structure validation
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