2v0o

From Proteopedia

(Difference between revisions)

Current revision

FCHO2 F-BAR domain

Structural highlights

2v0o is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FCHO2_HUMAN Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.^[1] ^[2] ^[3] ^[4]

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

A spectrum of membrane curvatures exists within cells, and proteins have evolved different modules to detect, create, and maintain these curvatures. Here we present the crystal structure of one such module found within human FCHo2. This F-BAR (extended FCH) module consists of two F-BAR domains, forming an intrinsically curved all-helical antiparallel dimer with a Kd of 2.5 microM. The module binds liposomes via a concave face, deforming them into tubules with variable diameters of up to 130 nm. Pulse EPR studies showed the membrane-bound dimer is the same as the crystal dimer, although the N-terminal helix changed conformation on membrane binding. Mutation of a phenylalanine on this helix partially attenuated narrow tubule formation, and resulted in a gain of curvature sensitivity. This structure shows a distant relationship to curvature-sensing BAR modules, and suggests how similar coiled-coil architectures in the BAR superfamily have evolved to expand the repertoire of membrane-sculpting possibilities.

Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.,Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT Structure. 2007 Jul;15(7):839-52. Epub 2007 Jun 1. PMID:17540576^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure. 2007 Jul;15(7):839-52. Epub 2007 Jun 1. PMID:17540576 doi:10.1016/j.str.2007.05.002
↑ Henne WM, Boucrot E, Meinecke M, Evergren E, Vallis Y, Mittal R, McMahon HT. FCHo proteins are nucleators of clathrin-mediated endocytosis. Science. 2010 Jun 4;328(5983):1281-4. PMID:20448150 doi:10.1126/science.1188462
↑ Uezu A, Umeda K, Tsujita K, Suetsugu S, Takenawa T, Nakanishi H. Characterization of the EFC/F-BAR domain protein, FCHO2. Genes Cells. 2011 Aug;16(8):868-78. PMID:21762413 doi:10.1111/j.1365-2443.2011.01536.x
↑ Mulkearns EE, Cooper JA. FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis. Mol Biol Cell. 2012 Apr;23(7):1330-42. doi: 10.1091/mbc.E11-09-0812. Epub 2012, Feb 9. PMID:22323290 doi:http://dx.doi.org/10.1091/mbc.E11-09-0812
↑ Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure. 2007 Jul;15(7):839-52. Epub 2007 Jun 1. PMID:17540576 doi:10.1016/j.str.2007.05.002

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/2v0o"

@@ Line 1: / Line 1: @@
-==FCHO2 F-BAR DOMAIN==
-<StructureSection load='2v0o' size='340' side='right' caption='[[2v0o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+==FCHO2 F-BAR domain==
+<StructureSection load='2v0o' size='340' side='right'caption='[[2v0o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v0o]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V0O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v0o]] is a 3 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=2V0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0O FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v0o RCSB], [http://www.ebi.ac.uk/pdbsum/2v0o PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0o OCA], [https://pdbe.org/2v0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0o RCSB], [https://www.ebi.ac.uk/pdbsum/2v0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0o ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FCHO2_HUMAN FCHO2_HUMAN] Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a lipid-binding activity with a preference for membranes enriched in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like the plasma membrane. Its membrane-bending activity might be important for the subsequent action of clathrin and adaptors in the formation of clathrin-coated vesicles. Involved in adaptor protein complex AP-2-dependent endocytosis of the transferrin receptor, it also functions in the AP-2-independent endocytosis of the LDL receptor.<ref>PMID:17540576</ref> <ref>PMID:20448150</ref> <ref>PMID:21762413</ref> <ref>PMID:22323290</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/v0/2v0o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v0o_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2v0o ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2v0o" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 29: / Line 34: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Evans, P R.]]
+[[Category: Large Structures]]
-[[Category: Henne, W M.]]
+[[Category: Evans PR]]
-[[Category: Kent, H M.]]
+[[Category: Henne WM]]
-[[Category: Mcmahon, H T.]]
+[[Category: Kent HM]]
-[[Category: Coiled-coil]]
+[[Category: McMahon HT]]
-[[Category: Efc domain]]
-[[Category: Endocytosis]]
-[[Category: Exocytosis]]
-[[Category: F-bar domain]]
-[[Category: Lipid- binding protein]]
-[[Category: Lipid-binding protein]]
-[[Category: Membrane curvature]]
-[[Category: Vesicle trafficking]]

2v0o

From Proteopedia

Current revision

FCHO2 F-BAR domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox