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2x3v

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Structure of The F-BAR Domain of Mouse Syndapin I

Structural highlights

2x3v is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.45Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PACN1_MOUSE May play a role in endocytosis.^[1]

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

Members of the Bin/amphiphysin/Rvs (BAR) domain protein superfamily are involved in membrane remodeling in various cellular pathways ranging from endocytic vesicle and T-tubule formation to cell migration and neuromorphogenesis. Membrane curvature induction and stabilization are encoded within the BAR or Fer-CIP4 homology-BAR (F-BAR) domains, alpha-helical coiled coils that dimerize into membrane-binding modules. BAR/F-BAR domain proteins often contain an SH3 domain, which recruits binding partners such as the oligomeric membrane-fissioning GTPase dynamin. How precisely BAR/F-BAR domain-mediated membrane deformation is regulated at the cellular level is unknown. Here we present the crystal structures of full-length syndapin 1 and its F-BAR domain. Our data show that syndapin 1 F-BAR-mediated membrane deformation is subject to autoinhibition by its SH3 domain. Release from the clamped conformation is driven by association of syndapin 1 SH3 with the proline-rich domain of dynamin 1, thereby unlocking its potent membrane-bending activity. We hypothesize that this mechanism might be commonly used to regulate BAR/F-BAR domain-induced membrane deformation and to potentially couple this process to dynamin-mediated fission. Our data thus suggest a structure-based model for SH3-mediated regulation of BAR/F-BAR domain function.

Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation.,Rao Y, Ma Q, Vahedi-Faridi A, Sundborger A, Pechstein A, Puchkov D, Luo L, Shupliakov O, Saenger W, Haucke V Proc Natl Acad Sci U S A. 2010 Apr 19. PMID:20404169^[2]

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

References

↑ Modregger J, Ritter B, Witter B, Paulsson M, Plomann M. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J Cell Sci. 2000 Dec;113 Pt 24:4511-21. PMID:11082044
↑ Rao Y, Ma Q, Vahedi-Faridi A, Sundborger A, Pechstein A, Puchkov D, Luo L, Shupliakov O, Saenger W, Haucke V. Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation. Proc Natl Acad Sci U S A. 2010 Apr 19. PMID:20404169

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/2x3v"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x3v' size='340' side='right'caption='[[2x3v]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x3v]] is a 3 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=2X3V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X3V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x3v]] is a 3 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=2X3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3V FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x3x|2x3x]], [[2x3w|2x3w]]</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]] 2.45&#8491;</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=2x3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3v OCA], [http://pdbe.org/2x3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x3v RCSB], [http://www.ebi.ac.uk/pdbsum/2x3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3v 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=2x3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3v OCA], [https://pdbe.org/2x3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3v RCSB], [https://www.ebi.ac.uk/pdbsum/2x3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3v ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PACN1_MOUSE PACN1_MOUSE]] May play a role in endocytosis.<ref>PMID:11082044</ref>
+[https://www.uniprot.org/uniprot/PACN1_MOUSE PACN1_MOUSE] May play a role in endocytosis.<ref>PMID:11082044</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Haucke, V]]
+[[Category: Haucke V]]
-[[Category: Ma, Q]]
+[[Category: Ma Q]]
-[[Category: Rao, Y]]
+[[Category: Rao Y]]
-[[Category: Saenger, W]]
+[[Category: Saenger W]]
-[[Category: Vahedi-Faridi, A]]
+[[Category: Vahedi-Faridi A]]
-[[Category: Bar]]
-[[Category: Dynamin]]
-[[Category: Endocytosis]]
-[[Category: N-wasp]]
-[[Category: Pacsin 1]]

2x3v

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Current revision

Structure of The F-BAR Domain of Mouse Syndapin I

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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