<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kosugi T</submitter><funding>NCRR NIH HHS</funding><pagination>498-503</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2856804</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>166(3)</volume><pubmed_abstract>The highly conserved DRY motif located at the end of the third transmembrane of G-protein-coupled receptors has been described as a key motif for several aspects of GPCR functions. However, in the case of the vertebrate gonadotropin-releasing hormone receptor (GnRHR), the amino acid in the third position in the DRY motif is variable. In the lamprey, a most basal vertebrate, the third amino acid of the "DRY" in lamprey (lGnRHR-1) is His, while it is most often His/Gln in the type II GnRHR. To investigate the functional significance of the substitution of DRY to DRH in the GnRHR-1, second messenger signaling, ligand binding and internalization of the wild-type and mutant lGnRH receptors were characterized with site-directed mutagenesis. Treatment of the DRE(151) and DRS(151) mutant receptors</pubmed_abstract><journal>General and comparative endocrinology</journal><pubmed_title>A role of Histidine151 in the lamprey gonadotropin-releasing hormone receptor-1 (lGnRHR-1): Functional insight of diverse amino acid residues in the position of Tyr of the DRY motif in GnRHR from an ancestral type II receptor.</pubmed_title><pmcid>PMC2856804</pmcid><funding_grant_id>R21 RR024477-02</funding_grant_id><funding_grant_id>5R21RR024477-02</funding_grant_id><funding_grant_id>R21 RR024477</funding_grant_id><pubmed_authors>Kosugi T</pubmed_authors><pubmed_authors>Sower SA</pubmed_authors></additional><is_claimable>false</is_claimable><name>A role of Histidine151 in the lamprey gonadotropin-releasing hormone receptor-1 (lGnRHR-1): Functional insight of diverse amino acid residues in the position of Tyr of the DRY motif in GnRHR from an ancestral type II receptor.</name><description>The highly conserved DRY motif located at the end of the third transmembrane of G-protein-coupled receptors has been described as a key motif for several aspects of GPCR functions. However, in the case of the vertebrate gonadotropin-releasing hormone receptor (GnRHR), the amino acid in the third position in the DRY motif is variable. In the lamprey, a most basal vertebrate, the third amino acid of the "DRY" in lamprey (lGnRHR-1) is His, while it is most often His/Gln in the type II GnRHR. To investigate the functional significance of the substitution of DRY to DRH in the GnRHR-1, second messenger signaling, ligand binding and internalization of the wild-type and mutant lGnRH receptors were characterized with site-directed mutagenesis. Treatment of the DRE(151) and DRS(151) mutant receptors</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 May</publication><modification>2025-04-19T23:55:20.611Z</modification><creation>2019-06-06T22:00:12Z</creation></dates><accession>S-EPMC2856804</accession><cross_references><pubmed>20005226</pubmed><doi>10.1016/j.ygcen.2009.12.001</doi></cross_references></HashMap>