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1d5f
From Proteopedia
(New page: 200px<br /> <applet load="1d5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5f, resolution 2.8Å" /> '''STRUCTURE OF AN E6AP...) |
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| - | [[Image:1d5f.gif|left|200px]]<br /> | + | [[Image:1d5f.gif|left|200px]]<br /><applet load="1d5f" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1d5f" size=" | + | |
caption="1d5f, resolution 2.8Å" /> | caption="1d5f, resolution 2.8Å" /> | ||
'''STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY'''<br /> | '''STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE 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== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1D5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1D5F is a [http://en.wikipedia.org/wiki/Single_protein 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=1D5F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[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 12:13:18 2008'' |
Revision as of 10:13, 21 February 2008
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STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY
Contents |
Overview
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
Known disease associated with this structure: Angelman syndrome OMIM:[601623]
About this Structure
1D5F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:13:18 2008
