4D01: Crystal Structure Of The Extracellular Domain Of The Human Alpha9 Nicotinic Acetylcholine Receptor

We determined the X-ray crystal structures of the extracellular domain (ECD) of the monomeric state of human neuronal alpha9 nicotinic acetylcholine receptor (nAChR) and of its complexes with the antagonists methyllycaconitine and alpha-bungarotoxin at resolutions of 1.8 A, 1.7 A and 2.7 A, respectively. The structure of the monomeric alpha9 ECD superimposed well with the structures of homologous proteins in pentameric assemblies, denoting native folding, despite the absence of a complementary subunit and transmembrane domain. The interaction motifs of both antagonists were similar to those in the complexes with homologous pentameric proteins, thus highlighting the major contribution of the principal side of alpha9 ECD to their binding. The structures revealed a functionally important beta7-beta10 strand interaction in alpha9-containing nAChRs, involving their unique Thr147, a hydration pocket similar to that of mouse alpha1 ECD and a membrane-facing network coordinated by the invariant Arg210.
PDB ID: 4D01Download
MMDB ID: 123526
PDB Deposition Date: 2014/4/23
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4D01: monomeric; determined by author and by software (PISA)
Molecular Components in 4D01
Label Count Molecule
Protein (1 molecule)
Neuronal Acetylcholine Receptor Subunit Alpha-9(Gene symbol: CHRNA9)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB