<p>There is a 48% amino acid identity of the entire subunit sequences. Within the ligand-binding domain, there is an 81% amino acid homology, with a 58% amino acid identity. Key residues for agonist binding are highlighted in yellow and mutated residues are in red. An * (asterisk) below residue alignment denotes positions that have a identical residues. A colon denotes groups with strongly similar properties and a scoring of >0.5 in the Gonnet PAM 250 matrix. A period denotes groups with weakly similar properties and a scoring of ≤0.5 in the Gonnet PAM 250 matrix <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0064685#pone.0064685-Pettersen1" target="_blank">[28]</a>.</p
<p>Structure-based sequence alignment of various NR LBDs shows that ligand pocket residues (boxed by...
<p>The amino acids in the bHLHZip domains of human c-MYC and human MYCN were aligned, while the seco...
<p>Loops A, B, and C, important in agonist binding in the nAChR α subunit, are underscored by a sing...
<p>A, Sequence alignment of monkey and human α6 subunits identified a single residue in the extracel...
<p>(A) Triple mutant D77T/L117Q/I196P: key agonist binding residues (yellow) and point mutations (re...
<p>Positions that are at least 30% or 95% conserved are highlighted in gray and black, respectively....
<p>(A) Alignment of protein sequences of the human ITSNs SH3 domains. The alignment was generated us...
<p>The amino acids showing sequence identity in both the receptors are shown as white text with blue...
<p>Predicted functional domains are depicted by arrows. Alignment and annotations were generated usi...
<p>The GluCl sequence was used as template for homology modeling throughout the GABA<sub>A</sub>R su...
Contains fulltext : 57293.pdf (publisher's version ) (Closed access)Literature stu...
<p>A: The residues with the mutations in the binding region (loops A (TYR93), and C (CYS191, LYS192,...
<p>Underlined is a putative assembly signal conserved in different GABA<sub>A</sub> receptor subunit...
Literature studies, 3D structure data, and a series of sequence analysis techniques were combined to...
<p>(A) Alignment of allatostatin-C receptor (AST-CR) I and II. (B) Alignment of pigment dispersing h...
<p>Structure-based sequence alignment of various NR LBDs shows that ligand pocket residues (boxed by...
<p>The amino acids in the bHLHZip domains of human c-MYC and human MYCN were aligned, while the seco...
<p>Loops A, B, and C, important in agonist binding in the nAChR α subunit, are underscored by a sing...
<p>A, Sequence alignment of monkey and human α6 subunits identified a single residue in the extracel...
<p>(A) Triple mutant D77T/L117Q/I196P: key agonist binding residues (yellow) and point mutations (re...
<p>Positions that are at least 30% or 95% conserved are highlighted in gray and black, respectively....
<p>(A) Alignment of protein sequences of the human ITSNs SH3 domains. The alignment was generated us...
<p>The amino acids showing sequence identity in both the receptors are shown as white text with blue...
<p>Predicted functional domains are depicted by arrows. Alignment and annotations were generated usi...
<p>The GluCl sequence was used as template for homology modeling throughout the GABA<sub>A</sub>R su...
Contains fulltext : 57293.pdf (publisher's version ) (Closed access)Literature stu...
<p>A: The residues with the mutations in the binding region (loops A (TYR93), and C (CYS191, LYS192,...
<p>Underlined is a putative assembly signal conserved in different GABA<sub>A</sub> receptor subunit...
Literature studies, 3D structure data, and a series of sequence analysis techniques were combined to...
<p>(A) Alignment of allatostatin-C receptor (AST-CR) I and II. (B) Alignment of pigment dispersing h...
<p>Structure-based sequence alignment of various NR LBDs shows that ligand pocket residues (boxed by...
<p>The amino acids in the bHLHZip domains of human c-MYC and human MYCN were aligned, while the seco...
<p>Loops A, B, and C, important in agonist binding in the nAChR α subunit, are underscored by a sing...