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| | <StructureSection load='5lpx' size='340' side='right'caption='[[5lpx]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5lpx' size='340' side='right'caption='[[5lpx]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lpx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LPX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LPX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lpx]] 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=5LPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LPX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5lpu|5lpu]]</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=5lpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lpx OCA], [https://pdbe.org/5lpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lpx RCSB], [https://www.ebi.ac.uk/pdbsum/5lpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lpx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lpx OCA], [http://pdbe.org/5lpx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lpx RCSB], [http://www.ebi.ac.uk/pdbsum/5lpx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lpx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ANXA2_HUMAN ANXA2_HUMAN]] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. | + | [https://www.uniprot.org/uniprot/ANXA2_HUMAN ANXA2_HUMAN] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ecsedi, P]] | + | [[Category: Ecsedi P]] |
| - | [[Category: Gogl, G]] | + | [[Category: Gogl G]] |
| - | [[Category: Kiss, B]] | + | [[Category: Kiss B]] |
| - | [[Category: Nyitray, L]] | + | [[Category: Nyitray L]] |
| - | [[Category: Calcium binding protein]]
| + | |
| - | [[Category: Phospho-mimickation]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| Structural highlights
Function
ANXA2_HUMAN Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response.
Publication Abstract from PubMed
Annexin A2 (ANXA2) has a versatile role in membrane-associated functions including membrane aggregation, endo- and exocytosis, and it is regulated by post-translational modifications and protein-protein interactions through the unstructured N-terminal domain (NTD). Our sequence analysis revealed a short motif responsible for clamping the NTD to the C-terminal core domain (CTD). Structural studies indicated that the flexibility of the NTD and CTD are interrelated and oppositely regulated by Tyr24 phosphorylation and Ser26Glu phosphomimicking mutation. The crystal structure of the ANXA2-S100A4 complex showed that asymmetric binding of S100A4 induces dislocation of the NTD from the CTD and, similar to the Ser26Glu mutation, unmasks the concave side of ANXA2. In contrast, pTyr24 anchors the NTD to the CTD and hampers the membrane-bridging function. This inhibition can be restored by S100A4 and S100A10 binding. Based on our results we provide a structural model for regulation of ANXA2-mediated membrane aggregation by NTD phosphorylation and S100 binding.
Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.,Ecsedi P, Kiss B, Gogl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vertessy B, Jeszenoi N, Hetenyi C, Schlosser G, Katona G, Nyitray L Structure. 2017 Aug 1;25(8):1195-1207.e5. doi: 10.1016/j.str.2017.06.001. Epub, 2017 Jun 29. PMID:28669632[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ecsedi P, Kiss B, Gogl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vertessy B, Jeszenoi N, Hetenyi C, Schlosser G, Katona G, Nyitray L. Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. Structure. 2017 Aug 1;25(8):1195-1207.e5. doi: 10.1016/j.str.2017.06.001. Epub, 2017 Jun 29. PMID:28669632 doi:http://dx.doi.org/10.1016/j.str.2017.06.001
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