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4fec

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Crystal Structure of Htt36Q3H

Structural highlights

4fec is a 3 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

HD_HUMAN Juvenile Huntington disease;Huntington disease. The disease is caused by mutations affecting the gene represented in this entry.

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.HD_HUMAN May play a role in microtubule-mediated transport or vesicle function.

Publication Abstract from PubMed

Huntington disease is an autosomal-dominant neurodegenerative disorder caused by a polyglutamine (polyQ) expansion (> 35Q) in the first exon (EX1) of huntingtin protein (Htt). mHtt protein is thought to adopt one or more toxic conformation(s) that are involved in pathogenic interactions in cells . However, the structure of mHtt is not known. Here, we present a near atomic resolution structure of mHtt36Q-EX1. To facilitate crystallization, three histidine residues (3H) were introduced within the Htt36Q stretch resulting in the sequence of Q 7HQHQHQ 27. The Htt36Q3H region adopts alpha-helix, loop, beta-hairpin conformations. Furthermore, we observed interactions between the backbone of the Htt36Q3H beta-strand with the aromatic residues mimicking putative-toxic interactions with other proteins. Our findings support previous predictions that the expanded mHtt-polyQ region adopts a beta-sheet structure. Detailed structural information about mHtt improves our understanding of the pathogenic mechanisms in HD and other polyQ expansion disorders and may form the basis for rational design of small molecules that target toxic conformations of disease-causing proteins.

Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues.,Kim M Prion. 2013 Jan 31;7(3). PMID:23370273^[1]

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

References

↑ Kim M. Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues. Prion. 2013 Jan 31;7(3). PMID:23370273

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4fec"

Categories: Escherichia coli K-12 | Homo sapiens | Large Structures | Kim M

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Htt36Q3H==
-<StructureSection load='4fec' size='340' side='right' caption='[[4fec]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='4fec' size='340' side='right'caption='[[4fec]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fec]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FEC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fec]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FEC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3io4|3io4]], [[3io6|3io6]], [[3iot|3iot]], [[3iou|3iou]], [[3ior|3ior]], [[4fe8|4fe8]], [[4feb|4feb]], [[4fed|4fed]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994, HD, HTT, IT15 ([http://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=4fec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fec OCA], [https://pdbe.org/4fec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fec RCSB], [https://www.ebi.ac.uk/pdbsum/4fec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fec ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fec RCSB], [http://www.ebi.ac.uk/pdbsum/4fec PDBsum]</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 ==
-[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[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 ==
@@ Line 18: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4fec" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Huntingtin|Huntingtin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Escherichia coli K-12]]
-[[Category: Kim, M]]
+[[Category: Homo sapiens]]
-[[Category: Alpha helix]]
+[[Category: Large Structures]]
-[[Category: Beta strand hairpin]]
+[[Category: Kim M]]
-[[Category: Beta-strand hairpin]]
-[[Category: Disease protein]]
-[[Category: Loop]]
-[[Category: Signaling protein]]

4fec

From Proteopedia

Current revision

Crystal Structure of Htt36Q3H

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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