2d3x: Difference between revisions
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[[ | ==THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327== | ||
<StructureSection load='2d3x' size='340' side='right'caption='[[2d3x]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
</table> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2d3x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Scott, D L]] | [[Category: Scott, D L]] | ||
Latest revision as of 13:27, 8 December 2021
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THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327THREE-DIMENSIONAL HOMOLOGY MODEL OF HUNTINGTIN RESIDUES 201- 327
Structural highlights
Publication Abstract from PubMedWe 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
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