1c4z: Difference between revisions
New page: left|200px<br /> <applet load="1c4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c4z, resolution 2.6Å" /> '''STRUCTURE OF E6AP: I... |
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[[Image:1c4z.gif|left|200px]]<br /> | [[Image:1c4z.gif|left|200px]]<br /><applet load="1c4z" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1c4z, resolution 2.6Å" /> | caption="1c4z, resolution 2.6Å" /> | ||
'''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY'''<br /> | '''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY'''<br /> | ||
==Overview== | ==Overview== | ||
The E6AP ubiquitin-protein ligase (E3) mediates the human | The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1C4Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http:// | 1C4Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4Z OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
[[Category: Beaudenon, S.]] | [[Category: Beaudenon, S.]] | ||
[[Category: Howley, P | [[Category: Howley, P M.]] | ||
[[Category: Huang, L.]] | [[Category: Huang, L.]] | ||
[[Category: Huibregtse, J | [[Category: Huibregtse, J M.]] | ||
[[Category: Kinnucan, E.]] | [[Category: Kinnucan, E.]] | ||
[[Category: Pavletich, N | [[Category: Pavletich, N P.]] | ||
[[Category: Wang, G.]] | [[Category: Wang, G.]] | ||
[[Category: bilobal structure]] | [[Category: bilobal structure]] | ||
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[[Category: elongated shape]] | [[Category: elongated shape]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:25 2008'' | ||
Revision as of 13:02, 21 February 2008
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STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY
OverviewOverview
The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3.
DiseaseDisease
Known disease associated with this structure: Angelman syndrome OMIM:[601623]
About this StructureAbout this Structure
1C4Z is a Protein complex structure of sequences from Homo sapiens. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
ReferenceReference
Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade., Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP, Science. 1999 Nov 12;286(5443):1321-6. PMID:10558980
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