5oo7: Difference between revisions
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The | ==The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)== | ||
<StructureSection load='5oo7' size='340' side='right' caption='[[5oo7]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5oo7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OO7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5oo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oo7 OCA], [http://pdbe.org/5oo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oo7 RCSB], [http://www.ebi.ac.uk/pdbsum/5oo7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oo7 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis. | |||
Epsin and Sla2 form assemblies through phospholipid interfaces.,Garcia-Alai MM, Heidemann J, Skruzny M, Gieras A, Mertens HDT, Svergun DI, Kaksonen M, Uetrecht C, Meijers R Nat Commun. 2018 Jan 23;9(1):328. doi: 10.1038/s41467-017-02443-x. PMID:29362354<ref>PMID:29362354</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5oo7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Garcia-Alai, M]] | [[Category: Garcia-Alai, M]] | ||
[[Category: Meijers, R]] | [[Category: Meijers, R]] | ||
[[Category: Adaptor protein complex]] | |||
[[Category: Endocytosis]] | |||
[[Category: Phospholipid binding]] | |||
Revision as of 08:00, 8 March 2018
The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)
Structural highlights
Publication Abstract from PubMedIn clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis. Epsin and Sla2 form assemblies through phospholipid interfaces.,Garcia-Alai MM, Heidemann J, Skruzny M, Gieras A, Mertens HDT, Svergun DI, Kaksonen M, Uetrecht C, Meijers R Nat Commun. 2018 Jan 23;9(1):328. doi: 10.1038/s41467-017-02443-x. PMID:29362354[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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