This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7tbz
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==The structure of ABCA1 Y482C== | ==The structure of ABCA1 Y482C== | ||
| - | <StructureSection load='7tbz' size='340' side='right'caption='[[7tbz]]' scene=''> | + | <StructureSection load='7tbz' size='340' side='right'caption='[[7tbz]], [[Resolution|resolution]] 4.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TBZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7tbz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TBZ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tbz OCA], [https://pdbe.org/7tbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tbz RCSB], [https://www.ebi.ac.uk/pdbsum/7tbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tbz ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tbz OCA], [https://pdbe.org/7tbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tbz RCSB], [https://www.ebi.ac.uk/pdbsum/7tbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tbz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/ABCA1_HUMAN ABCA1_HUMAN] Tangier disease;Apolipoprotein A-I deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ABCA1_HUMAN ABCA1_HUMAN] cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ATP-binding cassette transporter A1 (ABCA1) utilizes energy derived from ATP hydrolysis to export cholesterol and phospholipids from macrophages. ABCA1 plays a central role in the biosynthesis of high-density lipoprotein (HDL), which mediates reverse cholesterol transport and prevents detrimental lipid deposition. Mutations in ABCA1 cause Tangier disease characterized by a remarkable reduction in the amount of HDL in blood. Here we present cryo-electron microscopy structures of human ABCA1 in ATP-bound and nucleotide-free states. Structural comparison reveals that ATP molecules pull the nucleotide-binding domains together, inducing movements of transmembrane helices 1, 2, 7 and 8 through a series of salt-bridge interactions. Subsequently, extracellular domains (ECDs) undergo a rotation and introduce conformational changes in the ECD-transmembrane interface. In addition, while we observe a sterol-like molecule in ECDs, no such density was observed in the structure of an HDL-deficiency mutant ABCA1(Y482C), demonstrating the physiological importance of ECDs and a putative interaction mode between ABCA1 and its lipid acceptors. Thus, these structures, along with cholesterol efflux assays, advance the understanding ABCA1-mediated reverse cholesterol transport. | ||
| + | |||
| + | Cholesterol efflux mechanism revealed by structural analysis of human ABCA1 conformational states.,Sun Y, Li X Nat Cardiovasc Res. 2022;1(3):238-245. doi: 10.1038/s44161-022-00022-y. Epub 2022 , Mar 3. PMID:37181814<ref>PMID:37181814</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7tbz" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li X]] | [[Category: Li X]] | ||
[[Category: Sun Y]] | [[Category: Sun Y]] | ||
Current revision
The structure of ABCA1 Y482C
| |||||||||||
