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Example sentences for: achbp
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The crystal structure of two consecutive AChBP monomers [ 6 ] was used as a template to build a homology-model of four known native human nAChR subunit interfaces: alpha4-beta2 (I1), alpha4-beta4 (I2), alpha3-beta2 (I3), and alpha7-alpha7 (I4).
The AChBP displays a large amount of homology to the amino terminal of LGIC receptors and thus may be similar in structure [ 20 24 ] . The crystal structure of this protein reveals a loose 3 residue turn incorporating the conserved glycine residue [ 24 ] . Homologous residues in other LGIC subunits have also been identified and are shown in Figure 1. The residues identified in this study as altering binding affinity of 5-HT 3 R ligands would also be present on the same surface if this structure is present in the 5-HT 3 R. While Y140 lies somewhat outside the region identified by Chiara in the nAChR (homologous to γN107), γL109 and γL119 are homologous to Y142 and Y152 of the 5-HT 3AS R. The ability of lerisetron to interact with both Y142 and Y152 also supports the hypothesis that these two amino acids are present in a loop structure since the eight intervening residues would position Y142 and Y152 too far apart to permit them both to interact with a single ligand even if they were interacting with functional groups on opposite ends of the molecule.
All nAChR residues within 7A of the putative AChBP binding pocket described by Brejc et al.
In the center of this region is a critical glycine residue that is thought to play a role in establishing a hairpin loop [ 12 ] . Recent x-ray crystallographic data obtained from an ACh binding protein (AChBP) shows a loop structure in this region resulting from a 3 residue turn containing a glycine homologous to G147 of the 5-HT 3 R. On either side of this putative turn region are residues that have been identified as important to receptor binding [ 12 13 14 15 16 17 18 ] . The formation of this loop structure brings amino acids on either side of glycine into close proximity and may form a binding pocket that will accommodate one or more functional groups.
Based on the sequence alignment, the query sequences where threaded onto the first two subunits of the AChBP pentamer.
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