3s84

<StructureSection load='3s84' size='340' side='right' caption='[[3s84]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[3s84]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S84 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APOA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s84 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s84 RCSB], [http://www.ebi.ac.uk/pdbsum/3s84 PDBsum]</span></td></tr>

== 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>

 

[[Category: Davidson, W S]]

[[Category: Deng, X]]

[[Category: Thompson, T B]]

[[Category: Four helix bundle]]

[[Category: Transport protein]]