1eq1: Difference between revisions

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-{{Seed}}
-[[Image:1eq1.png|left|200px]]
-<!--
+==NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III==
-The line below this paragraph, containing "STRUCTURE_1eq1", creates the "Structure Box" on the page.
+<StructureSection load='1eq1' size='340' side='right'caption='[[1eq1]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1eq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQ1 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1eq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq1 OCA], [https://pdbe.org/1eq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1eq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eq1 ProSAT]</span></td></tr>
-{{STRUCTURE_1eq1|  PDB=1eq1  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/APL3_MANSE APL3_MANSE] Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eq/1eq1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eq1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The high-resolution NMR structure of apolipophorin III from the sphinx moth, Manduca sexta, has been determined in the lipid-free state. We show that lipid-free apolipophorin III adopts a unique helix-bundle topology that has several characteristic structural features. These include a marginally stable, up-and-down helix bundle that allows for concerted opening of the bundle about "hinged" loops upon lipid interaction and buried polar/ionizable residues and buried interhelical H-bonds located in the otherwise hydrophobic interior of the bundle that adjust protein stability and facilitate lipid-induced conformational opening. We suggest that these structural features modulate the conformational adaptability of the lipid-free helix bundle upon lipid binding and control return of the open conformation to the original lipid-free helix-bundle state. Taken together, these data provide a structural rationale for the ability of exchangeable apolipoproteins to reversibly interact with circulating lipoprotein particles.
-===NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III===
+Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein.,Wang J, Sykes BD, Ryan RO Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1188-93. Epub 2002 Jan 29. PMID:11818551<ref>PMID:11818551</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11818551}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1eq1" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11818551 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11818551}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-EQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ1 OCA].
-==Reference==
-Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein., Wang J, Sykes BD, Ryan RO, Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1188-93. Epub 2002 Jan 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11818551 11818551]
 [[Category: Manduca sexta]]
-[[Category: Single protein]]
+[[Category: Ryan RO]]
-[[Category: Ryan, R O.]]
+[[Category: Sykes BD]]
-[[Category: Sykes, B D.]]
+[[Category: Wang J]]
-[[Category: Wang, J.]]
-[[Category: Helix-short helix-helix recognition motif]]
-[[Category: Five helix-bundle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:36:48 2008''