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3io4

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Huntingtin amino-terminal region with 17 Gln residues - Crystal C90

Structural highlights

3io4 is a 3 chain structure with sequence from Escherichia coli O157:H7 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 3.63Å
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

HD_HUMAN May play a role in microtubule-mediated transport or vesicle function.MALE_ECO57 Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Huntington's disease is a genetic neurodegenerative disorder resulting from polyglutamine (polyQ) expansion (>36Q) within the first exon of Huntingtin (Htt) protein. We applied X-ray crystallography to determine the secondary structure of the first exon (EX1) of Htt17Q. The structure of Htt17Q-EX1 consists of an amino-terminal alpha helix, poly17Q region, and polyproline helix formed by the proline-rich region. The poly17Q region adopts multiple conformations in the structure, including alpha helix, random coil, and extended loop. The conformation of the poly17Q region is influenced by the conformation of neighboring protein regions, demonstrating the importance of the native protein context. We propose that the conformational flexibility of the polyQ region observed in our structure is a common characteristic of many amyloidogenic proteins. We further propose that the pathogenic polyQ expansion in the Htt protein increases the length of the random coil, which promotes aggregation and facilitates abnormal interactions with other proteins in cells.

Secondary structure of Huntingtin amino-terminal region.,Kim MW, Chelliah Y, Kim SW, Otwinowski Z, Bezprozvanny I Structure. 2009 Sep 9;17(9):1205-12. PMID:19748341^[1]

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

References

↑ Kim MW, Chelliah Y, Kim SW, Otwinowski Z, Bezprozvanny I. Secondary structure of Huntingtin amino-terminal region. Structure. 2009 Sep 9;17(9):1205-12. PMID:19748341 doi:10.1016/j.str.2009.08.002

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3io4"

@@ Line 3: / Line 3: @@
 <StructureSection load='3io4' size='340' side='right'caption='[[3io4]], [[Resolution|resolution]] 3.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3io4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IO4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3io4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] 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=3IO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IO4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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]] 3.63&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iot|3iot]], [[3io6|3io6]], [[3ior|3ior]], [[3iou|3iou]], [[3iov|3iov]], [[3iow|3iow]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3io4 OCA], [http://pdbe.org/3io4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3io4 RCSB], [http://www.ebi.ac.uk/pdbsum/3io4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3io4 ProSAT]</span></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=3io4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3io4 OCA], [https://pdbe.org/3io4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3io4 RCSB], [https://www.ebi.ac.uk/pdbsum/3io4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3io4 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 ==
-[[http://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+[https://www.uniprot.org/uniprot/HD_HUMAN HD_HUMAN] May play a role in microtubule-mediated transport or vesicle function.[https://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 38: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli O157:H7]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bezprozvanny, I]]
+[[Category: Bezprozvanny I]]
-[[Category: Chelliah, Y]]
+[[Category: Chelliah Y]]
-[[Category: Kim, M W]]
+[[Category: Kim MW]]
-[[Category: Kim, S W]]
+[[Category: Kim SW]]
-[[Category: Otwinowski, Z]]
+[[Category: Otwinowski Z]]
-[[Category: Apoptosis]]
-[[Category: Cytoplasm]]
-[[Category: Disease mutation]]
-[[Category: Hd]]
-[[Category: Htt18q-ex1]]
-[[Category: Huntingtin]]
-[[Category: Nucleus]]
-[[Category: Periplasm]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Signaling protein]]
-[[Category: Sugar transport]]
-[[Category: Transport]]
-[[Category: Triplet repeat expansion]]
-[[Category: Ubl conjugation]]

3io4

From Proteopedia

Current revision

Huntingtin amino-terminal region with 17 Gln residues - Crystal C90

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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