1uw5

From Proteopedia

(Difference between revisions)

Revision as of 13:01, 13 December 2023

Structure of PITP-alpha complexed to phosphatidylinositol

Structural highlights

1uw5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIPNA_HUMAN Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.

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

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.

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^[1]

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

References

↑ Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ. Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol. Structure. 2004 Feb;12(2):317-26. PMID:14962392 doi:10.1016/j.str.2004.01.013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uw5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1uw5' size='340' side='right'caption='[[1uw5]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uw5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOINOSITOL'>PIE</scene></td></tr>
+</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>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<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>
 <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>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PIPNA_HUMAN PIPNA_HUMAN]] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
+[https://www.uniprot.org/uniprot/PIPNA_HUMAN PIPNA_HUMAN] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Cockcroft, S]]
+[[Category: Cockcroft S]]
-[[Category: McDonald, N Q]]
+[[Category: McDonald NQ]]
-[[Category: Murray-Rust, J]]
+[[Category: Murray-Rust J]]
-[[Category: Skippen, A]]
+[[Category: Skippen A]]
-[[Category: Tilley, S J]]
+[[Category: Tilley SJ]]
-[[Category: Lipid-binding]]
-[[Category: Transfer protein]]
-[[Category: Transport]]

1uw5

From Proteopedia

Revision as of 13:01, 13 December 2023

Structure of PITP-alpha complexed to phosphatidylinositol

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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