1ioj

<StructureSection load='1ioj' size='340' side='right'caption='[[1ioj]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ioj]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOJ FirstGlance]. <br>

</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=1ioj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioj OCA], [https://pdbe.org/1ioj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ioj RCSB], [https://www.ebi.ac.uk/pdbsum/1ioj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ioj ProSAT]</span></td></tr>

[[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>

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== Publication Abstract from PubMed ==

The high-resolution conformation of human apoC-I in complexes with sodium dodecyl sulfate (SDS) is presented. As estimated from CD data, apoC-I adopts 54% helical secondary structure when bound to SDS, which is similar to the helical content previously found with phospholipids. The NMR-derived conformation of apoC-I is composed of two amphipathic helices, residues 7-29 and 38-52, separated by a flexible linker. The N-terminal helix contains a mobile hinge involving residues 12-15. The hydrophobic side chains cluster on the nonpolar face of both helices, thus forming two discrete lipid-binding sites in the N-terminal helix and one in the C-terminal helix. As suggested by amide proton resonance line widths and deuterium exchange rates, the N-terminal helix is more flexible and may bind less tightly to the detergent than the C-terminal helix. The different mobility of both helices appears to be related to side-chain composition, rather than length of the amphipathic helix, and may play a role in the function of apoC-I as an activator of lecithin:cholesterol acyltransferase (LCAT). A model is suggested in which the C-terminal helix serves as a lipid anchor while the N-terminal helix may hinge off the lipid surface to make specific contacts with LCAT.

Conformation of human apolipoprotein C-I in a lipid-mimetic environment determined by CD and NMR spectroscopy.,Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ Biochemistry. 1999 Nov 2;38(44):14475-84. PMID:10545169<ref>PMID:10545169</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ioj" style="background-color:#fffaf0;"></div>

[[Category: Cushley, R J]]

[[Category: Rozek, A]]

[[Category: Sparrow, J T]]

[[Category: Weisgraber, K H]]

[[Category: Lipid association]]