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1c4z

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(New page: 200px<br /> <applet load="1c4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c4z, resolution 2.6&Aring;" /> '''STRUCTURE OF E6AP: I...)
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[[Image:1c4z.gif|left|200px]]<br /><applet load="1c4z" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1c4z" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1c4z, resolution 2.6&Aring;" />
caption="1c4z, resolution 2.6&Aring;" />
'''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY'''<br />
'''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C4Z OCA].
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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.]]
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[[Category: Howley, P.M.]]
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[[Category: Howley, P M.]]
[[Category: Huang, L.]]
[[Category: Huang, L.]]
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[[Category: Huibregtse, J.M.]]
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[[Category: Huibregtse, J M.]]
[[Category: Kinnucan, E.]]
[[Category: Kinnucan, E.]]
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[[Category: Pavletich, N.P.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:17:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:25 2008''

Revision as of 10:02, 21 February 2008


1c4z, resolution 2.6Å

Drag the structure with the mouse to rotate

STRUCTURE OF E6AP: INSIGHTS INTO 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

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.

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

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