1ale: Difference between revisions

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{{Seed}}
[[Image:1ale.png|left|200px]]


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==CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY==
The line below this paragraph, containing "STRUCTURE_1ale", creates the "Structure Box" on the page.
<StructureSection load='1ale' size='340' side='right'caption='[[1ale]]' 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'>[[1ale]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALE 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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ale OCA], [https://pdbe.org/1ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ale RCSB], [https://www.ebi.ac.uk/pdbsum/1ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ale ProSAT]</span></td></tr>
{{STRUCTURE_1ale|  PDB=1ale  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/APOC1_HUMAN APOC1_HUMAN] Appears to modulate the interaction of APOE with beta-migrating VLDL and inhibit binding of beta-VLDL to the LDL receptor-related protein. Binds free fatty acids and reduces their intracellular esterification.<ref>PMID:17339654</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptides corresponding to the proposed lipid-binding domains of human apolipoprotein C-I, residues 7-24 (ALDKLKEFGNTLEDKARE) and 35-53 (SAKMREWFSETFQKVKEKL), were studied by CD and two-dimensional 1H NMR spectroscopy. Sodium dodecyl sulfate (SDS) was used to model the lipoprotein environment. Analysis of the CD data shows that both peptides lack well-defined structure in aqueous solution but adopt helical, ordered structures upon the addition of SDS. The helical nature of the peptides in the presence of SDS was confirmed by H alpha secondary shifts. A total of 199 (apoC-I(7-24)) and 266 (apoC-I(35-53)) distance restraints were used in distance geometry and simulated annealing calculations to generate average structures for both peptides in aqueous solutions containing SDS. The backbone (N, C alpha, C = O) RMSD from the average structure of an ensemble of 20 structures was 0.73 +/- 0.22 and 0.48 +/- 0.14 A for apoC-I(7-24) and apoC-I(35-53), respectively. In the presence of SDS, the distance geometry and simulated annealing calculations show that both peptides adopt well-defined amphipathic helices with distinct hydrophobic and hydrophilic faces. The calculated structures are discussed relative to predicted structures. Comparing our CD and NMR results for the apoC-I fragments in SDS with CD results of others obtained in the presence of dimyristoylphosphatidylcholine indicates that SDS may be a better model of the lipoprotein environment.


===CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY===
Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy.,Rozek A, Buchko GW, Cushley RJ Biochemistry. 1995 Jun 6;34(22):7401-8. PMID:7779782<ref>PMID:7779782</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_7779782}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1ale" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 7779782 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_7779782}}
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</StructureSection>
==About this Structure==
1ALE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALE OCA].
 
==Reference==
Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy., Rozek A, Buchko GW, Cushley RJ, Biochemistry. 1995 Jun 6;34(22):7401-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7779782 7779782]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Buchko, G W.]]
[[Category: Buchko GW]]
[[Category: Cushley, R J.]]
[[Category: Cushley RJ]]
[[Category: Rozek, A.]]
[[Category: Rozek A]]
[[Category: Apolipoprotein]]
 
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Retrieved from "https://proteopedia.org/1ale"