4BOO

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


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 42.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: TOMOGRAPHY 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure and Superorganization of Acetylcholine Receptor-Rapsyn Complexes.

Zuber, B.Unwin, N.

(2013) Proc Natl Acad Sci U S A 110: 10622

  • DOI: https://doi.org/10.1073/pnas.1301277110
  • Primary Citation of Related Structures:  
    4BOG, 4BOI, 4BON, 4BOO, 4BOR, 4BOT

  • 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.


  • Organizational Affiliation

    Laboratory of Experimental Morphology, Institute of Anatomy, University of Bern, CH-3000 Bern 9, Switzerland.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA
A, D
461Torpedo marmorataMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P02711 (Torpedo marmorata)
Explore P02711 
Go to UniProtKB:  P02711
Entity Groups  
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UniProt GroupP02711
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ACETYLCHOLINE RECEPTOR BETA SUBUNIT493Torpedo marmorataMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q6S3I0 (Torpedo marmorata)
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Go to UniProtKB:  Q6S3I0
Entity Groups  
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UniProt GroupQ6S3I0
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ACETYLCHOLINE RECEPTOR DELTA SUBUNIT522Torpedo marmorataMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q6S3H8 (Torpedo marmorata)
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Go to UniProtKB:  Q6S3H8
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UniProt GroupQ6S3H8
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ACETYLCHOLINE RECEPTOR GAMMA SUBUNIT505Torpedo marmorataMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q6S3H9 (Torpedo marmorata)
Explore Q6S3H9 
Go to UniProtKB:  Q6S3H9
Entity Groups  
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UniProt GroupQ6S3H9
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 42.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: TOMOGRAPHY 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIMOD
RECONSTRUCTIONPRIISM/IVE
RECONSTRUCTIONTOMO3D
RECONSTRUCTIONXmipp

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-06-26
    Type: Initial release
  • Version 1.1: 2013-07-10
    Changes: Database references
  • Version 1.2: 2017-08-02
    Changes: Data collection