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<article><div class="banner banner--gray banner--compact" style="--banner-background-image: url('/sites/default/files/media/image/2021-03/2015.jpg');--banner-background-focus: 50% 50%"><div class="banner__wrapper"><div class="banner__container"><h2 class="banner__heading">NIH Research Festival</h2><div class="banner__content"><p><strong><time datetime="2015-09-16">September 16</time> – <time datetime="2015-09-18">18, 2015</time></strong></p></div></div></div></div></article>
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<div class="section"><div data-drupal-messages-fallback class="hidden"></div></div><main role="main"><div id="main-content" tabindex="-1"></div><div class="section"><div class="content-sidebar"><div class="content-sidebar__main"><div class="content-sidebar__main-content"><div id="block-mainpagecontent-2"><article><h1>Investigating GPCR-ligand interaction by chemical crosslinking and mass spectrometry</h1><div class="schedule"><div class="schedule__label"><div class="schedule__label-text"><time datetime="2015-09-18">Friday, September 18, 2015</time>
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– Poster Session IV
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</div></div><div class="schedule__content"><div class="schedule__item"><div class="schedule__time">12:00 – 1:30 p.m.</div><div class="schedule__description"><p><strong>FAES Terrace</strong></p></div><div class="schedule__description"><p><strong>NIAAA</strong></p></div><div class="schedule__description"><p><strong>STRUCTBIO-5</strong></p></div></div></div></div><h2>Authors</h2><ul><li>BX Huang</li><li>J-W Lee</li><li>H-Y Kim</li></ul><h2>Abstract</h2><p>The orphan G protein-coupled receptor 110 (GPR110) belongs to the adhesion GPCR class that is distinctly characterized by the long N-terminus. We have recently identified a lipid ligand that interacts with GPR110. In an effort to understand the molecular basis of this GPCR-ligand interaction, we probe the conformational change of GPR110 using chemical crosslinking and mass spectrometry. Immunopurified HA-GPR110 (human) from HEK cells was treated with or without the ligand followed by incubation with disuccinimidyl suberate (DSS, a lysine-specific crosslinker). The samples were subjected to SDS-PAGE, tryptic digestion, nanoLC-ESI-MS/MS, and label-free quantitation. The MS-based approach identified thirteen through-space crosslinked lysine pairs in the N-terminal domain of the receptor, including K29-K38, K151-K73, K151-K254, K151-K442, K240-K187, K240-K254, K442-K240, K442-K254, K442-K398, K442-K427, K398-K427, K398-K438, and K427-K438. A through-space crosslinking between the intracellular loop 3 (K783) and the C-terminal (K852), along with two long-span loop-links (K864-K873 and K852-K860) within the C-terminal region, was also identified. The data indicated that the α-carbon distance of each of these crosslinked lysine pairs is within ~24 Å, the maximum crosslinking length of the crosslinker. Upon interacting with the lipid ligand, the crosslinking of K427-K438, K442-K427 and K398-K438 increased significantly, suggesting that the local structure of the N-terminal segment involving K427, K438, K398 and K442 becomes more folded upon the ligand binding. Our results represent the first experimental data for the three-dimensional structure of GPR110 at different stages. The ligand-induced change in the crosslinking profile provides valuable information for computer modeling or molecular dynamics simulations of the GPCR-ligand interaction.</p><p><strong>Scientific Focus Area</strong>: Structural Biology</p><p class="updated"><small>This page was last updated on Friday, March 26, 2021</small></p></article>
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