1l6l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1l6l" [edit=sysop:move=sysop])
Line 1: Line 1:
-
{{Seed}}
+
<table cellpadding='5'><tr><td style='background-color: yellow;border:2px solid black;font-size:150%;'>
-
{{Template:Murthy_fraud}}
+
WARNING: This structure was flagged as problematic. For additional information see '''2009, December:''' at [[Retractions and Fraud]].</td></tr></table>
-
[[Image:1l6l.png|left|200px]]
+
==Structures of Apolipoprotein A-II and a Lipid Surrogate Complex Provide Insights into Apolipoprotein-Lipid Interactions==
 +
<StructureSection load='1l6l' size='340' side='right' caption='[[1l6l]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1l6l]] is a 32 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=1L6L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L6L FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l6k|1l6k]]</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=1l6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l6l RCSB], [http://www.ebi.ac.uk/pdbsum/1l6l PDBsum]</span></td></tr>
 +
</table>
 +
== 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/l6/1l6l_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Apolipoproteins A-I and A-II form the major protein constituents of high-density lipid particles (HDL), the concentration of which is inversely correlated with the frequency of heart disease in humans. Although the physiological role of apolipoprotein A-II is unclear, evidence for its involvement in free fatty acid metabolism in mice has recently been obtained. Currently, the best characterized activity of apolipoprotein A-II is its potent antagonism of the anti-atherogenic and anti-inflammatory activities of apolipoprotein A-I, probably due to its competition with the latter for lipid acyl side chains in HDL. Many interactions of apolipoprotein A-I with enzymes and proteins involved in reverse cholesterol transport and HDL maturation are mediated by lipid-bound protein. The structural bases of interaction with lipids are expected to be common to exchangeable apolipoproteins and attributable to amphipathic alpha-helices present in each of them. Thus, characterization of apolipoprotein-lipid interactions in any apolipoprotein is likely to provide information that is applicable to the entire class. We report structures of human apolipoprotein A-II and its complex with beta-octyl glucoside, a widely used lipid surrogate. The former shows that disulfide-linked dimers of apolipoprotein A-II form amphipathic alpha-helices which aggregate into tetramers. Dramatic changes, observed in the presence of beta-octyl glucoside, might provide clues to the structural basis for its antagonism of apolipoprotein A-I. Additionally, excursions of individual molecules of apolipoprotein A-II from a common helical architecture in both structures indicate that lipid-bound apolipoproteins are likely to have an ensemble of related conformations. These structures provide the first experimental paradigm for description of apolipoprotein-lipid interactions at the atomic level.
-
<!--
+
Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions.,Kumar MS, Carson M, Hussain MM, Murthy HM Biochemistry. 2002 Oct 1;41(39):11681-91. PMID:12269810<ref>PMID:12269810</ref>
-
The line below this paragraph, containing "STRUCTURE_1l6l", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_1l6l| PDB=1l6l | SCENE= }}
+
-
===Structures of Apolipoprotein A-II and a Lipid Surrogate Complex Provide Insights into Apolipoprotein-Lipid Interactions===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
-
 
+
==See Also==
-
<!--
+
*[[Retractions and Fraud|Retractions and Fraud]]
-
The line below this paragraph, {{ABSTRACT_PUBMED_12269810}}, adds the Publication Abstract to the page
+
== References ==
-
(as it appears on PubMed at http://www.pubmed.gov), where 12269810 is the PubMed ID number.
+
<references/>
-
-->
+
__TOC__
-
{{ABSTRACT_PUBMED_12269810}}
+
</StructureSection>
-
 
+
-
==About this Structure==
+
-
1L6L is a 32 chains structure of sequences 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=1L6L OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:12269810</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Carson, M.]]
+
[[Category: Carson, M]]
-
[[Category: Hussain, M M.]]
+
[[Category: Hussain, M M]]
-
[[Category: Kumar, M S.]]
+
[[Category: Kumar, M S]]
-
[[Category: Murthy, H M.K.]]
+
[[Category: Murthy, H M.K]]
[[Category: Apolipoprotein]]
[[Category: Apolipoprotein]]
[[Category: Apolipoprotein a-ii]]
[[Category: Apolipoprotein a-ii]]
Line 35: Line 44:
[[Category: Helix]]
[[Category: Helix]]
[[Category: High density lipid]]
[[Category: High density lipid]]
-
 
+
[[Category: Lipid transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:02:00 2009''
+

Revision as of 08:28, 18 November 2014

WARNING: This structure was flagged as problematic. For additional information see 2009, December: at Retractions and Fraud.

Structures of Apolipoprotein A-II and a Lipid Surrogate Complex Provide Insights into Apolipoprotein-Lipid Interactions

1l6l, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA, Eric Martz

Personal tools