1eqx

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[[Image:1eqx.jpg|left|200px]]
 
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==SOLUTION STRUCTURE DETERMINATION AND MUTATIONAL ANALYSIS OF THE PAPILLOMAVIRUS E6-INTERACTING PEPTIDE OF E6AP==
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The line below this paragraph, containing "STRUCTURE_1eqx", creates the "Structure Box" on the page.
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<StructureSection load='1eqx' size='340' side='right'caption='[[1eqx]]' 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'>[[1eqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=1eqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqx OCA], [https://pdbe.org/1eqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eqx RCSB], [https://www.ebi.ac.uk/pdbsum/1eqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eqx ProSAT]</span></td></tr>
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{{STRUCTURE_1eqx| PDB=1eqx | SCENE= }}
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</table>
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== Disease ==
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'''SOLUTION STRUCTURE DETERMINATION AND MUTATIONAL ANALYSIS OF THE PAPILLOMAVIRUS E6-INTERACTING PEPTIDE OF E6AP'''
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[https://www.uniprot.org/uniprot/UBE3A_HUMAN UBE3A_HUMAN] Defects in UBE3A are a cause of Angelman syndrome (AS) [MIM:[https://omim.org/entry/105830 105830]; also known as 'happy puppet syndrome'. AS is characterized by features of severe motor and intellectual retardation, microcephaly, ataxia, frequent jerky limb movements and flapping of the arms and hands, hypotonia, hyperactivity, hypopigmentation, seizures, absence of speech, frequent smiling and episodes of paroxysmal laughter, and an unusual facies characterized by macrostomia, a large mandible and open-mouthed expression, a great propensity for protruding the tongue ('tongue thrusting'), and an occipital groove.<ref>PMID:10508479</ref> <ref>PMID:9585605</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/UBE3A_HUMAN UBE3A_HUMAN] E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo.<ref>PMID:10373495</ref> <ref>PMID:19325566</ref> <ref>PMID:19233847</ref> <ref>PMID:19204938</ref> <ref>PMID:19591933</ref> <ref>PMID:22645313</ref>
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==Overview==
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
E6AP is a cellular protein that binds cancer-related papillomaviral E6 proteins. The E6 binding domain, called E6ap, is located on an 18-amino acid segment of E6AP. The corresponding peptide was synthesized and its structure determined by nuclear magnetic resonance spectroscopy. The overall structure of the peptide is helical. A consensus E6-binding sequence among different E6 interacting proteins contains three conserved hydrophobic residues. In the structure of the E6AP peptide, the three conserved leucines (Leu 9, Leu 12, and Leu 13) form a hydrophobic patch on one face of the alpha-helix. Substitution of any of these leucines with alanine abolished binding to E6 protein, indicating that the entire hydrophobic patch is necessary. Mutation of a glutamate to proline, but not alanine, also disrupted the interaction between E6 and E6AP protein, suggesting that the E6-binding motif of the E6AP protein must be helical when bound to E6. Comparison of the E6ap structure and mutational results with those of another E6-binding protein (E6BP/ERC-55) indicates the existence of a general E6-binding motif.
E6AP is a cellular protein that binds cancer-related papillomaviral E6 proteins. The E6 binding domain, called E6ap, is located on an 18-amino acid segment of E6AP. The corresponding peptide was synthesized and its structure determined by nuclear magnetic resonance spectroscopy. The overall structure of the peptide is helical. A consensus E6-binding sequence among different E6 interacting proteins contains three conserved hydrophobic residues. In the structure of the E6AP peptide, the three conserved leucines (Leu 9, Leu 12, and Leu 13) form a hydrophobic patch on one face of the alpha-helix. Substitution of any of these leucines with alanine abolished binding to E6 protein, indicating that the entire hydrophobic patch is necessary. Mutation of a glutamate to proline, but not alanine, also disrupted the interaction between E6 and E6AP protein, suggesting that the E6-binding motif of the E6AP protein must be helical when bound to E6. Comparison of the E6ap structure and mutational results with those of another E6-binding protein (E6BP/ERC-55) indicates the existence of a general E6-binding motif.
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==About this Structure==
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Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP.,Be X, Hong Y, Wei J, Androphy EJ, Chen JJ, Baleja JD Biochemistry. 2001 Feb 6;40(5):1293-9. PMID:11170455<ref>PMID:11170455</ref>
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1EQX is a [[Single protein]] 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=1EQX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP., Be X, Hong Y, Wei J, Androphy EJ, Chen JJ, Baleja JD, Biochemistry. 2001 Feb 6;40(5):1293-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11170455 11170455]
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</div>
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<div class="pdbe-citations 1eqx" style="background-color:#fffaf0;"></div>
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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: Single protein]]
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[[Category: Large Structures]]
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[[Category: Androphy, E J.]]
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[[Category: Androphy EJ]]
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[[Category: Baleja, J D.]]
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[[Category: Baleja JD]]
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[[Category: Be, X.]]
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[[Category: Be X]]
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[[Category: Chen, J J.]]
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[[Category: Chen JJ]]
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[[Category: Hong, Y.]]
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[[Category: Hong Y]]
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[[Category: Alpha helix]]
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[[Category: Peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:25:26 2008''
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Current revision

SOLUTION STRUCTURE DETERMINATION AND MUTATIONAL ANALYSIS OF THE PAPILLOMAVIRUS E6-INTERACTING PEPTIDE OF E6AP

PDB ID 1eqx

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