1ln1

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{{Seed}}
 
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[[Image:1ln1.png|left|200px]]
 
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==Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine==
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The line below this paragraph, containing "STRUCTURE_1ln1", creates the "Structure Box" on the page.
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<StructureSection load='1ln1' size='340' side='right'caption='[[1ln1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ln1]] is a 1 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=1LN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LN1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#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=DLP:1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>DLP</scene></td></tr>
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{{STRUCTURE_1ln1| PDB=1ln1 | SCENE= }}
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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=1ln1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ln1 OCA], [https://pdbe.org/1ln1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ln1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ln1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ln1 ProSAT]</span></td></tr>
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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/1ln1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ln1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine===
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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:12055623<ref>PMID:12055623</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12055623}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ln1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12055623 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12055623}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1LN1 is a 1 chain 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=1LN1 OCA].
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==Reference==
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<ref group="xtra">PMID:12055623</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Agate, D S.]]
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[[Category: Large Structures]]
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[[Category: Chan, W W.]]
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[[Category: Agate DS]]
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[[Category: Cohen, D E.]]
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[[Category: Chan WW]]
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[[Category: Olsen, L R.]]
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[[Category: Cohen DE]]
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[[Category: Rajashankar, K R.]]
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[[Category: Olsen LR]]
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[[Category: Roderick, S L.]]
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[[Category: Rajashankar KR]]
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[[Category: Vetting, M W.]]
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[[Category: Roderick SL]]
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[[Category: Start domain]]
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[[Category: Vetting MW]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:15:57 2009''
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Current revision

Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine

PDB ID 1ln1

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