1uw5

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{{Seed}}
 
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[[Image:1uw5.png|left|200px]]
 
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==Structure of PITP-alpha complexed to phosphatidylinositol==
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The line below this paragraph, containing "STRUCTURE_1uw5", creates the "Structure Box" on the page.
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<StructureSection load='1uw5' size='340' side='right'caption='[[1uw5]], [[Resolution|resolution]] 2.90&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'>[[1uw5]] is a 4 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=1UW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UW5 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]] 2.9&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PIE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOINOSITOL'>PIE</scene></td></tr>
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{{STRUCTURE_1uw5| PDB=1uw5 | 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=1uw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uw5 OCA], [https://pdbe.org/1uw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1uw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uw5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIPNA_HUMAN PIPNA_HUMAN] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
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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/uw/1uw5_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=1uw5 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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Phosphatidylinositol transfer protein alpha (PITPalpha) selectively transports and promotes exchange of phosphatidylinositol (PI) and phosphatidylcholine (PC) between lipid bilayers. In higher eukaryotes PITPalpha is required for cellular functions such as phospholipase C-mediated signaling, regulated exocytosis, and secretory vesicle formation. We have determined the crystal structure of human PITPalpha bound to its physiological ligand, PI, at 2.95 A resolution. The structure identifies the critical side chains within the lipid-headgroup binding pocket that define the exquisite specificity for PI. Mutational analysis of the PI binding pocket is in good agreement with the structural data and allows manipulation of functional properties of PITPalpha. Surprisingly, there are no major conformational differences between PI- and PC-loaded PITPalpha, despite previous predictions. In the crystal, PITPalpha-PI is dimeric, with two identical dimers in the asymmetric unit. The dimer interface masks precisely the sequence we identify as contributing to PITPalpha membrane interaction. Our structure represents a soluble, transport-competent form of PI-loaded PITPalpha.
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===STRUCTURE OF PITP-ALPHA COMPLEXED TO PHOSPHATIDYLINOSITOL===
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Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol.,Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ Structure. 2004 Feb;12(2):317-26. PMID:14962392<ref>PMID:14962392</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_14962392}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1uw5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14962392 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14962392}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1UW5 is a [[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=1UW5 OCA].
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==Reference==
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Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol., Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ, Structure. 2004 Feb;12(2):317-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14962392 14962392]
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[[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: Cockcroft, S.]]
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[[Category: Cockcroft S]]
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[[Category: Mcdonald, N Q.]]
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[[Category: McDonald NQ]]
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[[Category: Murray-Rust, J.]]
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[[Category: Murray-Rust J]]
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[[Category: Skippen, A.]]
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[[Category: Skippen A]]
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[[Category: Tilley, S J.]]
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[[Category: Tilley SJ]]
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[[Category: Lipid-binding]]
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[[Category: Transfer protein]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:05:50 2008''
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Current revision

Structure of PITP-alpha complexed to phosphatidylinositol

PDB ID 1uw5

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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