1h0a

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[[Image:1h0a.jpg|left|200px]]<br /><applet load="1h0a" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h0a.jpg|left|200px]]
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caption="1h0a, resolution 1.70&Aring;" />
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'''EPSIN ENTH BOUND TO INS(1,4,5)P3'''<br />
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{{Structure
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|PDB= 1h0a |SIZE=350|CAPTION= <scene name='initialview01'>1h0a</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=DI1:I3p+Binding+Site+For+Chain+A'>DI1</scene>
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|LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene> and <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''EPSIN ENTH BOUND TO INS(1,4,5)P3'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H0A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=DIO:'>DIO</scene> and <scene name='pdbligand=I3P:'>I3P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=DI1:I3p+Binding+Site+For+Chain+A'>DI1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0A OCA].
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1H0A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0A OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12353027 12353027]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12353027 12353027]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: alpha-alpha superhelix]]
[[Category: alpha-alpha superhelix]]
[[Category: clathrin]]
[[Category: clathrin]]
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[[Category: coated vesicles]]
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[[Category: coated vesicle]]
[[Category: endocytosis]]
[[Category: endocytosis]]
[[Category: enth]]
[[Category: enth]]
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[[Category: triskelion]]
[[Category: triskelion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:31 2008''

Revision as of 09:30, 20 March 2008

Image:1h0a.jpg


PDB ID 1h0a

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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

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