View source for 6rmh


==The Rigid-body refined model of the normal Huntingtin.==
<StructureSection load='6rmh' size='340' side='right'caption='[[6rmh]], [[Resolution|resolution]] 9.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RMH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HTT, HD, IT15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6rmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rmh OCA], [https://pdbe.org/6rmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rmh RCSB], [https://www.ebi.ac.uk/pdbsum/6rmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rmh ProSAT]</span></td></tr>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/HD_HUMAN HD_HUMAN]] Juvenile Huntington disease;Huntington disease. The disease is caused by mutations affecting the gene represented in this entry. 
== Function ==
[[https://www.uniprot.org/uniprot/HD_HUMAN HD_HUMAN]] May play a role in microtubule-mediated transport or vesicle function. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural information on its HEAT-repeat domains. Here, we present analyses of the impact of polyQ length on the structure and function of HTT via an integrative structural and biochemical approach. The cryo-EM analysis of normal (Q23) and disease (Q78) type HTTs shows that the structures of apo HTTs significantly differ from the structure of HTT in a HAP40 complex and that the polyQ expansion induces global structural changes in the relative movements among the HTT domains. In addition, we show that the polyQ expansion alters the phosphorylation pattern across HTT and that Ser2116 phosphorylation in turn affects the global structure and function of HTT. These results provide a molecular basis for the effect of the polyQ segment on HTT structure and activity, which may be important for HTT pathology.

The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain.,Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ Structure. 2020 Sep 1;28(9):1035-1050.e8. doi: 10.1016/j.str.2020.06.008. Epub, 2020 Jul 14. PMID:32668197<ref>PMID:32668197</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rmh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Huntingtin|Huntingtin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Hebert, H]]
[[Category: Jung, T]]
[[Category: Perraro, M Dal]]
[[Category: Song, J]]
[[Category: Tamo, G]]
[[Category: Multivalent scaffold platform]]
[[Category: Protein binding]]