3lll

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{{STRUCTURE_3lll| PDB=3lll | SCENE= }}
 
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===Crystal structure of mouse pacsin2 F-BAR domain===
 
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{{ABSTRACT_PUBMED_20471395}}
 
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==Function==
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==Crystal structure of mouse pacsin2 F-BAR domain==
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[[http://www.uniprot.org/uniprot/PACN2_MOUSE PACN2_MOUSE]] May play a role in endocytosis.<ref>PMID:11082044</ref>
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<StructureSection load='3lll' size='340' side='right'caption='[[3lll]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PACN2_MOUSE PACN2_MOUSE] May play a role in endocytosis.<ref>PMID:11082044</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/3lll_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lll ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:20471395</ref>
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[[3lll]] is a 2 chain structure with sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020471395</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 3lll" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Rudolph, M G.]]
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[[Category: Rudolph MG]]
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[[Category: Coiled-coil]]
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[[Category: Cytoplasmic vesicle]]
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[[Category: Endocytosis]]
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[[Category: Membrane fusion]]
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[[Category: Phosphoprotein]]
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[[Category: Sh3 domain]]
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[[Category: Vesicular traffic]]
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Current revision

Crystal structure of mouse pacsin2 F-BAR domain

PDB ID 3lll

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