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| | ==Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1== | | ==Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1== |
| - | <StructureSection load='6nf3' size='340' side='right' caption='[[6nf3]], [[Resolution|resolution]] 2.33Å' scene=''> | + | <StructureSection load='6nf3' size='340' side='right'caption='[[6nf3]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nf3]] 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=6NF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NF3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NF3 FirstGlance]. <br> |
| - | </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=6nf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nf3 OCA], [http://pdbe.org/6nf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nf3 RCSB], [http://www.ebi.ac.uk/pdbsum/6nf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nf3 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33Å</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=6nf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nf3 OCA], [https://pdbe.org/6nf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nf3 RCSB], [https://www.ebi.ac.uk/pdbsum/6nf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nf3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Larson, S B]] | + | [[Category: Large Structures]] |
| - | [[Category: McPherson, A]] | + | [[Category: Larson SB]] |
| - | [[Category: Blood]] | + | [[Category: McPherson A]] |
| - | [[Category: Cholesterol]]
| + | |
| - | [[Category: Lipid binding protein]]
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| - | [[Category: Lipoprotein particle]]
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| - | [[Category: Vascular]]
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| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
Human apolipoprotein C1 (APOC1) is a 57 amino acid long polypeptide that through its potent inhibition of cholesterol ester transferase protein helps regulate the transfer of lipids between lipid particles. We have now determined the structure of APOC1 in four crystal forms by X-ray diffraction. A molecule of APOC1 is a single, slightly bent, alpha helix having 13 to 14 turns and a length of about 80 A. APOC1 exists as a dimer, but the dimers are not the same in the four crystals. In two monoclinic crystals, two helices closely engage one another in an anti-parallel fashion. The interactions between monomers are almost entirely hydrophobic with sparse electrostatic complements. In the third monoclinic crystal, the two monomers spread at one end of the dimer, like a scissor opening, and by translation along the crystallographic a axis, form a continuous, contiguous, sheet through the crystal. In the orthorhombic crystals two molecules of APOC1 are related by a non-crystallographic twofold axis to create an arc of about 120 A length. This symmetrical dimer utilizes interactions not present in dimers of the monoclinic crystals. Versatility of APOC1 monomer association shown by these crystals is suggestive of physiological function.
The Structure of Human Apolipoprotein C-1 in Four Different Crystal Forms.,McPherson A, Larson SB J Lipid Res. 2018 Dec 17. pii: jlr.M089441. doi: 10.1194/jlr.M089441. PMID:30559175[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Westerterp M, Berbee JF, Delsing DJ, Jong MC, Gijbels MJ, Dahlmans VE, Offerman EH, Romijn JA, Havekes LM, Rensen PC. Apolipoprotein C-I binds free fatty acids and reduces their intracellular esterification. J Lipid Res. 2007 Jun;48(6):1353-61. Epub 2007 Mar 5. PMID:17339654 doi:http://dx.doi.org/10.1194/jlr.M700024-JLR200
- ↑ McPherson A, Larson SB. The Structure of Human Apolipoprotein C-1 in Four Different Crystal Forms. J Lipid Res. 2018 Dec 17. pii: jlr.M089441. doi: 10.1194/jlr.M089441. PMID:30559175 doi:http://dx.doi.org/10.1194/jlr.M089441
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