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| | ==Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution== | | ==Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution== |
| - | <StructureSection load='1kcm' size='340' side='right' caption='[[1kcm]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1kcm' size='340' side='right'caption='[[1kcm]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kcm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KCM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kcm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KCM FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fvz|1fvz]]</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]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kcm OCA], [http://pdbe.org/1kcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kcm RCSB], [http://www.ebi.ac.uk/pdbsum/1kcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kcm ProSAT]</span></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=1kcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kcm OCA], [https://pdbe.org/1kcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kcm RCSB], [https://www.ebi.ac.uk/pdbsum/1kcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kcm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/PIPNA_MOUSE PIPNA_MOUSE]] Note=Defects in Pitpna are the cause of the vibrator phenotype which is characterized by early-onset progressive action tremor, degeneration of brain stem and spinal cord neurons, and juvenile death. The mutation is due to the insertion of an intracisternal A particle retrotransposon in intron 4 which results in a 5-fold reduction in protein levels. | + | [https://www.uniprot.org/uniprot/PIPNA_MOUSE PIPNA_MOUSE] Note=Defects in Pitpna are the cause of the vibrator phenotype which is characterized by early-onset progressive action tremor, degeneration of brain stem and spinal cord neurons, and juvenile death. The mutation is due to the insertion of an intracisternal A particle retrotransposon in intron 4 which results in a 5-fold reduction in protein levels. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PIPNA_MOUSE PIPNA_MOUSE]] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes. | + | [https://www.uniprot.org/uniprot/PIPNA_MOUSE PIPNA_MOUSE] Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Agianian, B]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gros, P]] | + | [[Category: Agianian B]] |
| - | [[Category: Kroon, J]] | + | [[Category: Gros P]] |
| - | [[Category: Schouten, A]] | + | [[Category: Kroon J]] |
| - | [[Category: Westerman, J]] | + | [[Category: Schouten A]] |
| - | [[Category: Wirtz, K W.A]] | + | [[Category: Westerman J]] |
| - | [[Category: Lipid binding protein]]
| + | [[Category: Wirtz KWA]] |
| - | [[Category: Phospholipid binding protein]]
| + | |
| - | [[Category: Phospholipid transport]]
| + | |
| - | [[Category: Pitp]]
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| Structural highlights
Disease
PIPNA_MOUSE Note=Defects in Pitpna are the cause of the vibrator phenotype which is characterized by early-onset progressive action tremor, degeneration of brain stem and spinal cord neurons, and juvenile death. The mutation is due to the insertion of an intracisternal A particle retrotransposon in intron 4 which results in a 5-fold reduction in protein levels.
Function
PIPNA_MOUSE 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 (PITP alpha) is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes in vitro and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. Here we report the three-dimensional crystal structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The structure reveals an open conformation characterized by a channel running through the protein. The channel is created by opening the phospholipid-binding cavity on one side by displacement of the C-terminal region and a hydrophobic lipid exchange loop, and on the other side by flattening of the central beta-sheet. The relaxed conformation is stabilized at the proposed membrane association site by hydrophobic interactions with a crystallographically related molecule, creating an intimate dimer. The observed open conformer is consistent with a membrane-bound state of PITP and suggests a mechanism for membrane anchoring and the presentation of phosphatidylinositol to kinases and phospholipases after its extraction from the membrane. Coordinates have been deposited in the Protein Data Bank (accession No. 1KCM).
Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association.,Schouten A, Agianian B, Westerman J, Kroon J, Wirtz KW, Gros P EMBO J. 2002 May 1;21(9):2117-21. PMID:11980708[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schouten A, Agianian B, Westerman J, Kroon J, Wirtz KW, Gros P. Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association. EMBO J. 2002 May 1;21(9):2117-21. PMID:11980708 doi:http://dx.doi.org/10.1093/emboj/21.9.2117
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