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| | ==Crystal structure of the PH domain of Evectin-2 from human== | | ==Crystal structure of the PH domain of Evectin-2 from human== |
| - | <StructureSection load='3via' size='340' side='right' caption='[[3via]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3via' size='340' side='right'caption='[[3via]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3via]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VIA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3via]] 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=3VIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VIA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aj4|3aj4]]</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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLEKHB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3via FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3via OCA], [https://pdbe.org/3via PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3via RCSB], [https://www.ebi.ac.uk/pdbsum/3via PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3via ProSAT]</span></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=3via FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3via OCA], [http://pdbe.org/3via PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3via RCSB], [http://www.ebi.ac.uk/pdbsum/3via PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3via ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PKHB2_HUMAN PKHB2_HUMAN]] Involved in retrograde transport of recycling endosomes.<ref>PMID:21911378</ref> <ref>PMID:22281740</ref> | + | [https://www.uniprot.org/uniprot/PKHB2_HUMAN PKHB2_HUMAN] Involved in retrograde transport of recycling endosomes.<ref>PMID:21911378</ref> <ref>PMID:22281740</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Evectin-2 is a recycling endosomal protein involved in retrograde transport. Its primary sequence contains an N-terminal pleckstrin homology (PH) domain and a C-terminal hydrophobic region. The PH domain of evectin-2 can specifically bind phosphatidylserine, which is enriched in recycling endosomes, and plays an essential role in retrograde transport from recycling endosomes to the trans-Golgi network. The structure of human evectin-2 PH domain in complex with O-phospho-L-serine has recently been reported and demonstrates how the head group of phosphatidylserine is recognized. However, it was not possible to elucidate from the structure why evectin-2 cannot bind phosphatidic acid or phosphatidylethanolamine, which share a common moiety with phosphatidylserine. Here, the crystal structure at 1.75 A resolution of an apo form of human evectin-2 PH domain, in which the ligand-binding site is free from crystal packing and is thus appropriate for comparison with the structure of the complex, is reported. Comparison between the structures of the apo form and the O-phospho-L-serine complex revealed ligand-induced conformational change evoked by interaction between the carboxyl moiety of the head group of phosphatidylserine and the main-chain N atom of Thr14. This structural change effectively explains the strict ligand specificity of the PH domain of human evectin-2.
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| - | Structural basis of the strict phospholipid binding specificity of the pleckstrin homology domain of human evectin-2.,Okazaki S, Kato R, Uchida Y, Taguchi T, Arai H, Wakatsuki S Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):117-23. Epub 2012, Jan 13. PMID:22281740<ref>PMID:22281740</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3via" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kato, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Okazaki, S]] | + | [[Category: Kato R]] |
| - | [[Category: Wakatsuki, S]] | + | [[Category: Okazaki S]] |
| - | [[Category: Antiparallel beta sheet]] | + | [[Category: Wakatsuki S]] |
| - | [[Category: Protein transport]]
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| Structural highlights
Function
PKHB2_HUMAN Involved in retrograde transport of recycling endosomes.[1] [2]
References
- ↑ Uchida Y, Hasegawa J, Chinnapen D, Inoue T, Okazaki S, Kato R, Wakatsuki S, Misaki R, Koike M, Uchiyama Y, Iemura S, Natsume T, Kuwahara R, Nakagawa T, Nishikawa K, Mukai K, Miyoshi E, Taniguchi N, Sheff D, Lencer WI, Taguchi T, Arai H. Intracellular phosphatidylserine is essential for retrograde membrane traffic through endosomes. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15846-51. Epub 2011 Sep 12. PMID:21911378 doi:10.1073/pnas.1109101108
- ↑ Okazaki S, Kato R, Uchida Y, Taguchi T, Arai H, Wakatsuki S. Structural basis of the strict phospholipid binding specificity of the pleckstrin homology domain of human evectin-2. Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):117-23. Epub 2012, Jan 13. PMID:22281740 doi:10.1107/S0907444911051626
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