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1ln3

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(New page: 200px<br /> <applet load="1ln3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ln3, resolution 2.90&Aring;" /> '''Structure of Human ...)
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[[Image:1ln3.gif|left|200px]]<br />
 
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<applet load="1ln3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ln3, resolution 2.90&Aring;" />
 
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'''Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)'''<br />
 
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==Overview==
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==Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)==
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Phosphatidylcholines (PtdChos) comprise the most common phospholipid class, in eukaryotic cells. In mammalian cells, these insoluble molecules are, transferred between membranes by a highly specific phosphatidylcholine, transfer protein (PC-TP) belonging to the steroidogenic acute regulatory, protein related transfer (START) domain superfamily of hydrophobic, ligand-binding proteins. The crystal structures of human PC-TP in complex, with dilinoleoyl-PtdCho or palmitoyl-linoleoyl-PtdCho reveal that a single, well-ordered PtdCho molecule occupies a centrally located tunnel. The, positively charged choline headgroup of the lipid engages in cation-pi, interactions within a cage formed by the faces of three aromatic residues., These binding determinants and those for the phosphoryl group may be, exposed to the lipid headgroup at the membrane-water interface by a, conformational change involving the amphipathic C-terminal helix and an, Omega-loop. The structures presented here provide a basis for, rationalizing the specificity of PC-TP for PtdCho and may identify common, features used by START proteins to bind their hydrophobic ligands.
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<StructureSection load='1ln3' size='340' side='right'caption='[[1ln3]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ln3]] 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=1LN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LN3 FirstGlance]. <br>
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1LN3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CPL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LN3 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPL:1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>CPL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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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=1ln3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ln3 OCA], [https://pdbe.org/1ln3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ln3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ln3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ln3 ProSAT]</span></td></tr>
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Structure of human phosphatidylcholine transfer protein in complex with its ligand., Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE, Nat Struct Biol. 2002 Jul;9(7):507-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12055623 12055623]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPCT_HUMAN PPCT_HUMAN] Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule.<ref>PMID:12055623</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/ln/1ln3_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=1ln3 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: Agate, D.S.]]
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[[Category: Agate DS]]
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[[Category: Chan, W.W.]]
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[[Category: Chan WW]]
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[[Category: Cohen, D.E.]]
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[[Category: Cohen DE]]
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[[Category: Olsen, L.R.]]
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[[Category: Olsen LR]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar KR]]
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[[Category: Roderick, S.L.]]
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[[Category: Roderick SL]]
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[[Category: Vetting, M.W.]]
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[[Category: Vetting MW]]
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[[Category: CPL]]
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[[Category: start domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:02:44 2007''
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Current revision

Structure of Human Phosphatidylcholine Transfer Protein in Complex with Palmitoyl-Linoleoyl Phosphatidylcholine (Seleno-Met Protein)

PDB ID 1ln3

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