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1i5j

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Revision as of 09:37, 2 January 2015

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

Structural highlights

1i5j is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[APOC2_HUMAN] Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:207750]. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.^[1]

Function

[APOC2_HUMAN] Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.

NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.,MacRaild CA, Hatters DM, Howlett GJ, Gooley PR Biochemistry. 2001 May 8;40(18):5414-21. PMID:11331005^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Inadera H, Hibino A, Kobayashi J, Kanzaki T, Shirai K, Yukawa S, Saito Y, Yoshida S. A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama). Biochem Biophys Res Commun. 1993 Jun 30;193(3):1174-83. PMID:8323539 doi:http://dx.doi.org/S0006-291X(83)71749-3
↑ MacRaild CA, Hatters DM, Howlett GJ, Gooley PR. NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate. Biochemistry. 2001 May 8;40(18):5414-21. PMID:11331005

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i5j"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1i5j]] is a 1 chain structure with 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=1I5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I5J FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i5j RCSB], [http://www.ebi.ac.uk/pdbsum/1i5j PDBsum]</span></td></tr>
+</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=1i5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i5j RCSB], [http://www.ebi.ac.uk/pdbsum/1i5j PDBsum]</span></td></tr>
-<table>
+</table>
 == Disease ==
 [[http://www.uniprot.org/uniprot/APOC2_HUMAN APOC2_HUMAN]] Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:[http://omim.org/entry/207750 207750]]. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.<ref>PMID:8323539</ref>
@@ Line 32: / Line 32: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Gooley, P R.]]
+[[Category: Gooley, P R]]
-[[Category: Hatters, D M.]]
+[[Category: Hatters, D M]]
-[[Category: Howlett, G J.]]
+[[Category: Howlett, G J]]
-[[Category: MacRaild, C A.]]
+[[Category: MacRaild, C A]]
 [[Category: Amphipathic alpha helix]]
 [[Category: Lipid transport]]
 [[Category: Protein-lipid interaction]]

1i5j

From Proteopedia

Revision as of 09:37, 2 January 2015

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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