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1x03

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Revision as of 16:31, 27 October 2021

Crystal structure of endophilin BAR domain

Structural highlights

1x03 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1x04
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SH3G2_HUMAN] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.

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

The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 A, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.

Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.,Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N EMBO J. 2006 Jun 21;25(12):2889-97. Epub 2006 Jun 8. PMID:16763557^[1]

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

References

↑ Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 2006 Jun 21;25(12):2889-97. Epub 2006 Jun 8. PMID:16763557

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/1x03"

@@ Line 3: / Line 3: @@
 <StructureSection load='1x03' size='340' side='right'caption='[[1x03]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x03]] is a 1 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=1X03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X03 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x03]] is a 1 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=1X03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X03 FirstGlance]. <br>
 </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x04|1x04]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x04|1x04]]</div></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=1x03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x03 OCA], [http://pdbe.org/1x03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x03 RCSB], [http://www.ebi.ac.uk/pdbsum/1x03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x03 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=1x03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x03 OCA], [https://pdbe.org/1x03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x03 RCSB], [https://www.ebi.ac.uk/pdbsum/1x03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x03 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SH3G2_HUMAN SH3G2_HUMAN]] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.
+[[https://www.uniprot.org/uniprot/SH3G2_HUMAN SH3G2_HUMAN]] Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1x03

From Proteopedia

Revision as of 16:31, 27 October 2021

Crystal structure of endophilin BAR domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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