3s84: Difference between revisions

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<StructureSection load='3s84' size='340' side='right'caption='[[3s84]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3s84' size='340' side='right'caption='[[3s84]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3s84]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S84 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3s84]] is a 2 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=3S84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S84 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APOA4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3s84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s84 OCA], [https://pdbe.org/3s84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s84 RCSB], [https://www.ebi.ac.uk/pdbsum/3s84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s84 ProSAT]</span></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=3s84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s84 OCA], [https://pdbe.org/3s84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s84 RCSB], [https://www.ebi.ac.uk/pdbsum/3s84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s84 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/APOA4_HUMAN APOA4_HUMAN]] May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.  
[https://www.uniprot.org/uniprot/APOA4_HUMAN APOA4_HUMAN] May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Apolipoproteins are key structural elements of lipoproteins and critical mediators of lipid metabolism. Their detergent-like properties allow them to emulsify lipid or exist in a soluble lipid-free form in various states of self-association. Unfortunately, these traits have hampered high-resolution structural studies needed to understand the biogenesis of cardioprotective high-density lipoproteins (HDLs). We derived a crystal structure of the core domain of human apolipoprotein (apo)A-IV, an HDL component and important mediator of lipid absorption. The structure at 2.4 A depicts two linearly connected 4-helix bundles participating in a helix swapping arrangement that offers a clear explanation for how the protein self-associates as well as clues to the structure of its monomeric form. This also provides a logical basis for antiparallel arrangements recently described for lipid-containing particles. Furthermore, we propose a "swinging door" model for apoA-IV lipid association.
 
The Structure of Dimeric Apolipoprotein A-IV and Its Mechanism of Self-Association.,Deng X, Morris J, Dressmen J, Tubb MR, Tso P, Jerome WG, Davidson WS, Thompson TB Structure. 2012 May 9;20(5):767-79. PMID:22579246<ref>PMID:22579246</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3s84" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davidson, W S]]
[[Category: Davidson WS]]
[[Category: Deng, X]]
[[Category: Deng X]]
[[Category: Thompson, T B]]
[[Category: Thompson TB]]
[[Category: Four helix bundle]]
[[Category: Transport protein]]