1h0a

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[[Image:1h0a.jpg|left|200px]]
[[Image:1h0a.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1h0a |SIZE=350|CAPTION= <scene name='initialview01'>1h0a</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1h0a", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=DI1:I3p+Binding+Site+For+Chain+A'>DI1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1h0a| PDB=1h0a | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0a OCA], [http://www.ebi.ac.uk/pdbsum/1h0a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h0a RCSB]</span>
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}}
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'''EPSIN ENTH BOUND TO INS(1,4,5)P3'''
'''EPSIN ENTH BOUND TO INS(1,4,5)P3'''
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[[Category: Ford, M G.J.]]
[[Category: Ford, M G.J.]]
[[Category: Mcmahon, H T.]]
[[Category: Mcmahon, H T.]]
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[[Category: 4]]
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[[Category: Alpha-alpha superhelix]]
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[[Category: 5)p3]]
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[[Category: Clathrin]]
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[[Category: alpha-alpha superhelix]]
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[[Category: Coated vesicle]]
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[[Category: clathrin]]
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[[Category: Endocytosis]]
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[[Category: coated vesicle]]
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[[Category: Enth]]
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[[Category: endocytosis]]
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[[Category: Epsin]]
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[[Category: enth]]
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[[Category: Triskelion]]
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[[Category: epsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:15:02 2008''
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[[Category: ins(1]]
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[[Category: triskelion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:55:13 2008''
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Revision as of 15:15, 2 May 2008

Template:STRUCTURE 1h0a

EPSIN ENTH BOUND TO INS(1,4,5)P3


Overview

Clathrin-mediated endocytosis involves cargo selection and membrane budding into vesicles with the aid of a protein coat. Formation of invaginated pits on the plasma membrane and subsequent budding of vesicles is an energetically demanding process that involves the cooperation of clathrin with many different proteins. Here we investigate the role of the brain-enriched protein epsin 1 in this process. Epsin is targeted to areas of endocytosis by binding the membrane lipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)). We show here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P(2) in conjunction with clathrin polymerization. We have discovered that formation of an amphipathic alpha-helix in epsin is coupled to PtdIns(4,5)P(2) binding. Mutation of residues on the hydrophobic region of this helix abolishes the ability to curve membranes. We propose that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature. On lipid monolayers epsin alone is sufficient to facilitate the formation of clathrin-coated invaginations.

About this Structure

1H0A is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Curvature of clathrin-coated pits driven by epsin., Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT, Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027 Page seeded by OCA on Fri May 2 18:15:02 2008

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