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| | ==structure of mouse syndapin I (crystal form 2)== | | ==structure of mouse syndapin I (crystal form 2)== |
| - | <StructureSection load='2x3w' size='340' side='right' caption='[[2x3w]], [[Resolution|resolution]] 2.64Å' scene=''> | + | <StructureSection load='2x3w' size='340' side='right'caption='[[2x3w]], [[Resolution|resolution]] 2.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x3w]] is a 4 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=2X3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x3w]] is a 4 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=2X3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X3W FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x3v|2x3v]], [[2x3x|2x3x]]</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]] 2.64Å</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=2x3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3w OCA], [http://pdbe.org/2x3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x3w RCSB], [http://www.ebi.ac.uk/pdbsum/2x3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3w 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=2x3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x3w OCA], [https://pdbe.org/2x3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x3w RCSB], [https://www.ebi.ac.uk/pdbsum/2x3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x3w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Haucke, V]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ma, Q]] | + | [[Category: Haucke V]] |
| - | [[Category: Rao, Y]] | + | [[Category: Ma Q]] |
| - | [[Category: Saenger, W]] | + | [[Category: Rao Y]] |
| - | [[Category: Dynamin]]
| + | [[Category: Saenger W]] |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: N-wasp]]
| + | |
| - | [[Category: Pacsin i]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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
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