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| | ==Crystal structure of mouse pacsin2 F-BAR domain== | | ==Crystal structure of mouse pacsin2 F-BAR domain== |
| - | <StructureSection load='3lll' size='340' side='right' caption='[[3lll]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='3lll' size='340' side='right'caption='[[3lll]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lll]] is a 2 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=3LLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LLL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lll]] is a 2 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=3LLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LLL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pacsin2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3lll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lll OCA], [http://pdbe.org/3lll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lll RCSB], [http://www.ebi.ac.uk/pdbsum/3lll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lll 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=3lll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lll OCA], [https://pdbe.org/3lll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lll RCSB], [https://www.ebi.ac.uk/pdbsum/3lll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lll ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PACN2_MOUSE PACN2_MOUSE]] May play a role in endocytosis.<ref>PMID:11082044</ref> | + | [https://www.uniprot.org/uniprot/PACN2_MOUSE PACN2_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: Rudolph, M G]] | + | [[Category: Mus musculus]] |
| - | [[Category: Coiled-coil]] | + | [[Category: Rudolph MG]] |
| - | [[Category: Cytoplasmic vesicle]]
| + | |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: Membrane fusion]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Vesicular traffic]]
| + | |
| Structural highlights
Function
PACN2_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
The protein kinase C and casein kinase 2 substrates in neurons (PACSINs) represent a subfamily of membrane-binding proteins characterized by an amino-terminal Bin-Amphiphysin-Rvs (F-BAR) domain. PACSINs link membrane trafficking with actin dynamics and regulate the localization of distinct cargo molecules. The F-BAR domain forms a dimer essential for lipid binding. We have obtained crystals of authentic murine PACSIN 2 that contain an ordered F-BAR domain, indicating that additional domains are flexibly connected to F-BAR. The structure shares similarity to other BAR domains and exhibits special features unique to PACSINs. These include the uneven distribution of charged residues on the concave molecular surface and a so-called wedge loop that is driven into the membrane upon binding of PACSIN. The murine PACSIN 2 F-BAR domain requires dimerization for sensing of curved membranes, and the present structure also provides a mechanism for higher-order oligomer formation. Importantly, comparison of murine with human and Drosophila PACSIN 2 F-BAR domains reveals stark differences in the orientation of distal helical segments leading to a wider crescent shape of murine PACSIN 2. We define hinge residues for these movements that may help PACSINs sense and concomitantly reinforce membrane curvature.
A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing.,Plomann M, Wittmann JG, Rudolph MG J Mol Biol. 2010 Jul 9;400(2):129-36. Epub 2010 May 13. PMID:20471395[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
- ↑ Plomann M, Wittmann JG, Rudolph MG. A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing. J Mol Biol. 2010 Jul 9;400(2):129-36. Epub 2010 May 13. PMID:20471395 doi:10.1016/j.jmb.2010.05.008
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