3h1d

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[[Image:3h1d.jpg|left|200px]]
 
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==Structure of the HUWE1 HECT Domain==
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The line below this paragraph, containing "STRUCTURE_3h1d", creates the "Structure Box" on the page.
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<StructureSection load='3h1d' size='340' side='right'caption='[[3h1d]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3h1d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H1D FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.892&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3h1d| PDB=3h1d | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h1d OCA], [https://pdbe.org/3h1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h1d RCSB], [https://www.ebi.ac.uk/pdbsum/3h1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h1d ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HUWE1_HUMAN HUWE1_HUMAN] Defects in HUWE1 are the cause of mental retardation syndromic X-linked Turner type (MRXST) [MIM:[https://omim.org/entry/300706 300706]; also known as mental retardation and macrocephaly syndrome. MRXST shows clinical variability. Associated phenotypes include macrocephaly and variable contractures. A chromosomal microduplication involving HUWE1 and HSD17B10 is the cause of mental retardation X-linked type 17 (MRX17) [MIM:[https://omim.org/entry/300705 300705]; also known as mental retardation X-linked type 31 (MRX31). Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation.<ref>PMID:18252223</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HUWE1_HUMAN HUWE1_HUMAN] E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation.<ref>PMID:15989956</ref> <ref>PMID:15989957</ref> <ref>PMID:15767685</ref> <ref>PMID:15567145</ref> <ref>PMID:17567951</ref> <ref>PMID:18488021</ref> <ref>PMID:19713937</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/3h1d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h1d ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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E3 ubiquitin ligases catalyze the final step of ubiquitin conjugation and regulate numerous cellular processes. The HECT class of E3 ubiquitin (Ub) ligases directly transfers Ub from bound E2 enzyme to a myriad of substrates. The catalytic domain of HECT Ub ligases has a bilobal architecture that separates the E2 binding region and catalytic site. An important question regarding HECT domain function is the control of ligase activity and specificity. Here we present a functional analysis of the HECT domain of the E3 ligase HUWE1 based on crystal structures and show that a single N-terminal helix significantly stabilizes the HECT domain. We observe that this element modulates HECT domain activity, as measured by self-ubiquitination induced in the absence of this helix, as distinct from its effects on Ub conjugation of substrate Mcl-1. Such subtle changes to the protein may be at the heart of the vast spectrum of substrate specificities displayed by HECT domain E3 ligases.
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===Structure of the HUWE1 HECT Domain===
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A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities.,Pandya RK, Partridge JR, Love KR, Schwartz TU, Ploegh HL J Biol Chem. 2010 Feb 19;285(8):5664-73. Epub 2009 Dec 10. PMID:20007713<ref>PMID:20007713</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3h1d" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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3H1D is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H1D OCA].
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Partridge, J R.]]
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[[Category: Large Structures]]
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[[Category: Schwartz, T U.]]
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[[Category: Partridge JR]]
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[[Category: Alternative splicing]]
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[[Category: Schwartz TU]]
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[[Category: Chromosomal rearrangement]]
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[[Category: Cytoplasm]]
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[[Category: Differentiation]]
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[[Category: Disease mutation]]
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[[Category: Dna-binding]]
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[[Category: E3ligase]]
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[[Category: Hect]]
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[[Category: Ligase]]
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[[Category: Lobe]]
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[[Category: Mental retardation]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Ubiquitin]]
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[[Category: Ubl conjugation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 9 15:54:28 2009''
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Current revision

Structure of the HUWE1 HECT Domain

PDB ID 3h1d

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