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| <StructureSection load='3haj' size='340' side='right'caption='[[3haj]], [[Resolution|resolution]] 2.78Å' scene=''> | | <StructureSection load='3haj' size='340' side='right'caption='[[3haj]], [[Resolution|resolution]] 2.78Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3haj]] is a 2 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=3HAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3haj]] is a 2 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=3HAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HAJ 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></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]] 2.78Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hah|3hah]], [[3hai|3hai]]</div></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></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PACSIN2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3haj OCA], [https://pdbe.org/3haj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3haj RCSB], [https://www.ebi.ac.uk/pdbsum/3haj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3haj 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=3haj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3haj OCA], [https://pdbe.org/3haj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3haj RCSB], [https://www.ebi.ac.uk/pdbsum/3haj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3haj ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/PACN2_HUMAN PACN2_HUMAN]] May play a role in endocytosis.
| + | [https://www.uniprot.org/uniprot/PACN2_HUMAN PACN2_HUMAN] May play a role in endocytosis. |
| == 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: Human]] | + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Navarro, M V.A S]] | + | [[Category: Navarro MVAS]] |
- | [[Category: Peng, G]] | + | [[Category: Peng G]] |
- | [[Category: Rajashankar, K R]] | + | [[Category: Rajashankar KR]] |
- | [[Category: Sondermann, H]] | + | [[Category: Sondermann H]] |
- | [[Category: Wang, Q]] | + | [[Category: Wang Q]] |
- | [[Category: Alternative splicing]]
| + | |
- | [[Category: Coiled coil]]
| + | |
- | [[Category: Cytoplasmic vesicle]]
| + | |
- | [[Category: Endocytosis]]
| + | |
- | [[Category: F-bar]]
| + | |
- | [[Category: Fap52]]
| + | |
- | [[Category: Pacsin]]
| + | |
- | [[Category: Phosphoprotein]]
| + | |
- | [[Category: Polymorphism]]
| + | |
- | [[Category: Sh3 domain]]
| + | |
- | [[Category: Syndapin]]
| + | |
| Structural highlights
Function
PACN2_HUMAN May play a role in endocytosis.
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
Peripheral membrane proteins of the Bin/amphiphysin/Rvs (BAR) and Fer-CIP4 homology-BAR (F-BAR) family participate in cellular membrane trafficking and have been shown to generate membrane tubules. The degree of membrane bending appears to be encoded in the structure and immanent curvature of the particular protein domains, with BAR and F-BAR domains inducing high- and low-curvature tubules, respectively. In addition, oligomerization and the formation of ordered arrays influences tubule stabilization. Here, the F-BAR domain-containing protein Pacsin was found to possess a unique activity, creating small tubules and tubule constrictions, in addition to the wide tubules characteristic for this subfamily. Based on crystal structures of the F-BAR domain of Pacsin and mutagenesis studies, vesiculation could be linked to the presence of unique structural features distinguishing it from other F-BAR proteins. Tubulation was suppressed in the context of the full-length protein, suggesting that Pacsin is autoinhibited in solution. The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis beyond their role as scaffold proteins.
Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin.,Wang Q, Navarro MV, Peng G, Molinelli E, Lin Goh S, Judson BL, Rajashankar KR, Sondermann H Proc Natl Acad Sci U S A. 2009 Jun 24. PMID:19549836[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang Q, Navarro MV, Peng G, Molinelli E, Lin Goh S, Judson BL, Rajashankar KR, Sondermann H. Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc Natl Acad Sci U S A. 2009 Jun 24. PMID:19549836
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