2d3x: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:2d3x.png|left|200px]]


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==THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327==
The line below this paragraph, containing "STRUCTURE_2d3x", creates the "Structure Box" on the page.
<StructureSection load='2d3x' size='340' side='right'caption='[[2d3x]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D3X FirstGlance]. <br>
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</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=2d3x FirstGlance], [https://www.ebi.ac.uk/pdbsum/2d3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d3x ProSAT]</span></td></tr>
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{{STRUCTURE_2d3x|  PDB=2d3x  |  SCENE=  }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have identified a domain in the N terminus of huntingtin that binds to membranes. A three-dimensional homology model of the structure of the binding domain predicts helical HEAT repeats, which emanate a positive electrostatic potential, consistent with a charge-based mechanism for membrane association. An amphipathic helix capable of inserting into pure lipid bilayers may serve to anchor huntingtin to the membrane. In cells, N-terminal huntingtin fragments targeted to regions of plasma membrane enriched in phosphatidylinositol 4,5-bisphosphate, receptor bound-transferrin, and endogenous huntingtin. N-terminal huntingtin fragments with an expanded polyglutamine tract aberrantly localized to intracellular regions instead of plasma membrane. Our data support a new model in which huntingtin directly binds membranes through electrostatic interactions with acidic phospholipids.


===THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327===
Huntingtin associates with acidic phospholipids at the plasma membrane.,Kegel KB, Sapp E, Yoder J, Cuiffo B, Sobin L, Kim YJ, Qin ZH, Hayden MR, Aronin N, Scott DL, Isenberg G, Goldmann WH, DiFiglia M J Biol Chem. 2005 Oct 28;280(43):36464-73. Epub 2005 Aug 5. PMID:16085648<ref>PMID:16085648</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_16085648}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3X OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:16085648</ref><references group="xtra"/>
[[Category: Scott, D L]]
[[Category: Scott, D L]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:19:02 2010''

Latest revision as of 13:27, 8 December 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

We have identified a domain in the N terminus of huntingtin that binds to membranes. A three-dimensional homology model of the structure of the binding domain predicts helical HEAT repeats, which emanate a positive electrostatic potential, consistent with a charge-based mechanism for membrane association. An amphipathic helix capable of inserting into pure lipid bilayers may serve to anchor huntingtin to the membrane. In cells, N-terminal huntingtin fragments targeted to regions of plasma membrane enriched in phosphatidylinositol 4,5-bisphosphate, receptor bound-transferrin, and endogenous huntingtin. N-terminal huntingtin fragments with an expanded polyglutamine tract aberrantly localized to intracellular regions instead of plasma membrane. Our data support a new model in which huntingtin directly binds membranes through electrostatic interactions with acidic phospholipids.

Huntingtin associates with acidic phospholipids at the plasma membrane.,Kegel KB, Sapp E, Yoder J, Cuiffo B, Sobin L, Kim YJ, Qin ZH, Hayden MR, Aronin N, Scott DL, Isenberg G, Goldmann WH, DiFiglia M J Biol Chem. 2005 Oct 28;280(43):36464-73. Epub 2005 Aug 5. PMID:16085648[1]

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

References

  1. ↑ Kegel KB, Sapp E, Yoder J, Cuiffo B, Sobin L, Kim YJ, Qin ZH, Hayden MR, Aronin N, Scott DL, Isenberg G, Goldmann WH, DiFiglia M. Huntingtin associates with acidic phospholipids at the plasma membrane. J Biol Chem. 2005 Oct 28;280(43):36464-73. Epub 2005 Aug 5. PMID:16085648 doi:10.1074/jbc.M503672200
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