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1opp

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[[Image:1opp.jpg|left|200px]]<br /><applet load="1opp" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1opp" />
 
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'''PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES'''<br />
 
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==Overview==
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==PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES==
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A peptide comprising the N-terminal 38 residues of human apolipoprotein, C-I (apoC-I(1-38)) was synthesized using solid-phase methods and its, solution conformation studied by CD and 1H NMR spectroscopy. The CD data, indicate that apoC-I(1-38) has a similar helical content (55%) in the, presence of saturating amounts of SDS or egg yolk lysophosphatidylcholine., A structural ensemble of SDS-bound apoC-I(1-38) was calculated from 464, NOE-based distance restraints using distance geometry methods., ApoC-I(1-38) adopts a helical structure between residues V4 and K30 and an, extended C-terminus from Q31 when associated with SDS. The region K12-G15, undergoes slow conformational exchange as indicated by above-average amide, resonance linewidths, large temperature coefficients, and fast exchange (&lt;, 2 h) of backbone amide protons with deuterium. The mobility of K12-G15 is, reflected in the poorly defined dihedral angles of K12 and E13 in the, calculated ensemble of structures. The average structure of apoC-I(1-38), is curved toward its hydrophobic face with bends of 125 degrees, centered, at K12/E13, and 150 degrees, centered at K21. This curvature appears to be, driven by the interaction of two hydrophobic clusters, one formed by, residues L8, L11, F14, and L18, and the other by L25, I26, and I29, with, the amphiphile SDS. Based on our present structural definition of, apoC-I(1-38) and the previously obtained structure of the fragment, apoC-I(35-53), we propose the secondary structure of intact apolipoprotein, C-I.
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<StructureSection load='1opp' size='340' side='right'caption='[[1opp]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1opp]] 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=1OPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPP FirstGlance]. <br>
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1OPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1OPP OCA].
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</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=1opp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opp OCA], [https://pdbe.org/1opp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opp RCSB], [https://www.ebi.ac.uk/pdbsum/1opp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opp ProSAT]</span></td></tr>
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==Reference==
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</table>
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Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and 1H NMR spectroscopy., Rozek A, Buchko GW, Kanda P, Cushley RJ, Protein Sci. 1997 Sep;6(9):1858-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9300485 9300485]
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/op/1opp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1opp ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Buchko, G.W.]]
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[[Category: Buchko GW]]
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[[Category: Cushley, R.J.]]
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[[Category: Cushley RJ]]
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[[Category: Kanda, P.]]
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[[Category: Kanda P]]
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[[Category: Rozek, A.]]
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[[Category: Rozek A]]
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[[Category: amphipathic helix]]
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[[Category: apolipoprotein]]
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[[Category: lcat activation]]
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[[Category: lipid association]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:35:05 2008''
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Current revision

PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES

PDB ID 1opp

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