1c4z: Difference between revisions
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[[Image:1c4z.gif|left|200px]] | [[Image:1c4z.gif|left|200px]] | ||
'''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY''' | {{Structure | ||
|PDB= 1c4z |SIZE=350|CAPTION= <scene name='initialview01'>1c4z</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C4Z is a [ | 1C4Z is a [[Protein complex]] structure of sequences 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=1C4Z OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10558980 10558980] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: elongated shape]] | [[Category: elongated shape]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:50 2008'' | ||
Revision as of 11:19, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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