3sh1

Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR

spinqualitylabelsall models 3sh1, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sh1 is a 10 chain structure with sequence from Aplysia californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ACT, BMA, MG, MLK, MPD, MRD, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8WSF8_APLCA Publication Abstract from PubMed 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 alpha7 nAChR. These chimeric proteins exhibit a shift in affinities to reflect alpha7 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 alpha7 nAChR glycosylation site. Creating an alpha7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: crystallographic and ligand selectivity analyses.,Nemecz A, Taylor P J Biol Chem. 2011 Dec 9;286(49):42555-65. Epub 2011 Oct 18. PMID:22009746 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetylcholine binding protein 3D structures

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