1nd7
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ubiquitin ligases (E3) select proteins for ubiquitylation, a modification | + | Ubiquitin ligases (E3) select proteins for ubiquitylation, a modification that directs altered subcellular trafficking and/or degradation of the target protein. HECT domain E3 ligases not only recognize, but also directly catalyze, ligation of ubiquitin to their protein substrates. The crystal structure of the HECT domain of the human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP. While the individual N and C lobes of WWP1 possess very similar folds to those of E6AP, the organization of the two lobes relative to one another is different from E6AP due to a rotation about a polypeptide hinge linking the N and C lobes. Mutational analyses suggest that a range of conformations achieved by rotation about this hinge region is essential for catalytic activity. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bowman, M | + | [[Category: Bowman, M E.]] |
| - | [[Category: Ferrer, J | + | [[Category: Ferrer, J L.]] |
[[Category: Hunter, T.]] | [[Category: Hunter, T.]] | ||
| - | [[Category: Joaziero, C | + | [[Category: Joaziero, C A.P.]] |
| - | [[Category: Noel, J | + | [[Category: Noel, J P.]] |
| - | [[Category: Verdecia, M | + | [[Category: Verdecia, M A.]] |
| - | [[Category: Wells, N | + | [[Category: Wells, N J.]] |
[[Category: e3]] | [[Category: e3]] | ||
[[Category: hect]] | [[Category: hect]] | ||
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[[Category: wwp1]] | [[Category: wwp1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:50 2008'' |
Revision as of 12:04, 21 February 2008
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Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase
Overview
Ubiquitin ligases (E3) select proteins for ubiquitylation, a modification that directs altered subcellular trafficking and/or degradation of the target protein. HECT domain E3 ligases not only recognize, but also directly catalyze, ligation of ubiquitin to their protein substrates. The crystal structure of the HECT domain of the human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP. While the individual N and C lobes of WWP1 possess very similar folds to those of E6AP, the organization of the two lobes relative to one another is different from E6AP due to a rotation about a polypeptide hinge linking the N and C lobes. Mutational analyses suggest that a range of conformations achieved by rotation about this hinge region is essential for catalytic activity.
About this Structure
1ND7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase., Verdecia MA, Joazeiro CA, Wells NJ, Ferrer JL, Bowman ME, Hunter T, Noel JP, Mol Cell. 2003 Jan;11(1):249-59. PMID:12535537
Page seeded by OCA on Thu Feb 21 14:04:50 2008
Categories: Homo sapiens | Single protein | Bowman, M E. | Ferrer, J L. | Hunter, T. | Joaziero, C A.P. | Noel, J P. | Verdecia, M A. | Wells, N J. | E3 | Hect | Ligase | Ubiquitin | Wwp1
