Words similar to achbp
Example sentences for: achbp
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The interaction is included in the model based on structural information obtained from the crystal structure of AChBP [ 27 ] . The region of this protein homologous to loop E and loop D of the 5-HT 3A receptor suggests a loop structure from Y140 to Y152 and a 3-residue turn containing a glycine at position 147 and the β-strand from W89 through Y93 oriented as shown in Figure 6. The orientation of lerisetron between W89 and Y142A as shown would enable the N-benzyl group to be positioned in close proximity to R91.
We also docked HEPES to the receptors, since this ligand was found in the crystal structure of AChBP.
Sequence alignment of mouse 5-HT 3 AR, α7 nAchR and AChBP result in alignment of the proposed D and E loop of the 5-HT 3 AR with corresponding regions of the α7 nAchR and AChBP.
Previous reports have shown on other systems that a single-residue mutation in a receptor is sufficient for the development of specific ligands [ 13 14 ] . Based on the recent crystal structure of AChBP, we could propose a detailed description of the structural variations of nAChR subtypes.
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.
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