3SIO

Ac-AChBP ligand binding domain (not including beta 9-10 linker) mutated to human alpha-7 nAChR

Summary for 3SIO

• Entry DOI: 10.2210/pdb3sio/pdb
• Related: 2BYR 3SH1 3T4M
• Descriptor: Soluble acetylcholine receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: mutated acetylcholine binding protein, aplysia californica, alpha-7 human nicotinic acetylcholine receptor, achbp, nachr, binding protein, acetylcholine, glycosylation, receptor, methyllycaconitine
• Biological source: Aplysia californica (California sea hare)
• Total number of polymer chains: 10
• Total formula weight: 277709.07

Authors

Nemecz, A.,Taylor, P.W. (deposition date: 2011-06-19, release date: 2011-10-26, Last modification date: 2024-11-06)

Primary citation

Nemecz, A.,Taylor, P.
Creating an alpha-7 nicotinic acetylcholine recognition domain from the acetylcholine binding protein: crystallographic and ligand selectivity analyses
J.Biol.Chem., 286:42555-42565, 2011

PubMed Abstract: Determining the structure of the ligand-binding domain of the nicotinic acetylcholine receptor (nAChR) has been a long standing goal in the design of selective drugs useful in implicated diseases for this prevalent receptor family. Acetylcholine-binding proteins have proven to be valuable surrogates with structural similarity and sequence identity to the extracellular domain of the nicotinic receptor, yet these soluble proteins have their unique features and do not serve as exact replicates of the nAChRs of interest. Here we systematically modify the sequence of these proteins toward the homomeric human α7 nAChR. These chimeric proteins exhibit a shift in affinities to reflect α7 binding characteristics yet maintain expression levels and stability conducive for crystallization. We also present a pentameric humanoid nAChR extracellular domain with the structural determination of the α7 nAChR glycosylation site.

PubMed: 22009746
DOI: 10.1074/jbc.M111.286583

Experimental method

X-RAY DIFFRACTION (2.32 Å)