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3lll

From Proteopedia

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Current revision

Crystal structure of mouse pacsin2 F-BAR domain

Structural highlights

3lll is a 2 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 3.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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/3lll"

Categories: Large Structures | Mus musculus | Rudolph MG

@@ Line 1: / Line 1: @@
 ==Crystal structure of mouse pacsin2 F-BAR domain==
-<StructureSection load='3lll' size='340' side='right' caption='[[3lll]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+<StructureSection load='3lll' size='340' side='right'caption='[[3lll]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == 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]] 3.3&#8491;</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>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/3lll_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/3lll_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 33: / Line 33: @@
 __TOC__
 </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]]

3lll

From Proteopedia

Current revision

Crystal structure of mouse pacsin2 F-BAR domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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