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<title>Use of disulfide crosslinking to monitor movement of ATP sites during ATP hydrolysis cycle of the human P-glycoprotein (ABCB1) | NIH Research Festival</title>
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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>Use of disulfide crosslinking to monitor movement of ATP sites during ATP hydrolysis cycle of the human P-glycoprotein (ABCB1)</h1><div class="schedule"><div class="schedule__label"><div class="schedule__label-text"><time datetime="2015-09-16">Wednesday, September 16, 2015</time>
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– Poster Session I
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</div></div><div class="schedule__content"><div class="schedule__item"><div class="schedule__time">3:30 – 5:00 p.m.</div><div class="schedule__description"><p><strong>FAES Terrace</strong></p></div><div class="schedule__description"><p><strong>NCI</strong></p></div><div class="schedule__description"><p><strong>MOLBIO-25</strong></p></div></div></div></div><h2>Authors</h2><ul><li>A Mobin</li><li>S Shukla</li><li>SV Ambudkar</li></ul><h2>Abstract</h2><p>P-glycoprotein (P-gp, ABCB1), which is linked to cancer multidrug resistance, transports a variety of amphipathic chemically dissimilar compounds including anticancer drugs out of cells by using the energy from ATP hydrolysis. The mechanism linking ATP hydrolysis to the transport cycle of P-gp still remains unclear. An oxidative crosslinker, copper-1-10-phenenthroline (Cu-phe), was used to elucidate the conformational states of P-gp during its catalytic cycle. Of the seven cysteine residues located at various positions within P-gp, C431 and C1074, located within the Walker A motifs of nucleotide-binding domains (NBDs) could be cross-linked in the presence of Cu-Phe. Therefore, we used these residues as reporter sites to study the conformational changes associated with the catalytic cycle of P-gp. Cu-phe was not able to crosslink wild-type (WT) P-gp in the ADP-vanadate trapped conformation. However, partial crosslinking of an ATP hydrolysis-defective mutant of P-gp (E556Q/E1201Q) was observed. In addition, ADP alone did not inhibit the crosslinking of WT P-gp, while AMP-PNP, ADP-vanadate and AMP-PNP-vanadate were able to inhibit the crosslinking induced by Cu-Phe for WT P-gp. This was in contrast to the E556Q/E1201Q mutant, for which, a partial crosslinking was observed in the presence of all nucleotides, irrespective of the presence or absence of vanadate, suggesting that the conformation of E556Q/E1201Q mutant NBDs might be different compared to WT NBDs. The data in aggregate demonstrate that crosslinking of cysteine residues induced by Cu-phe can be used to probe conformational changes in ATP sites during the ATP hydrolysis cycle of P-gp.</p><p><strong>Scientific Focus Area</strong>: Molecular Biology and Biochemistry</p><p class="updated"><small>This page was last updated on Friday, March 26, 2021</small></p></article>
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