1nd7

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{{STRUCTURE_1nd7| PDB=1nd7 | SCENE= }}
{{STRUCTURE_1nd7| PDB=1nd7 | SCENE= }}
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'''Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase'''
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===Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12535537 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12535537}}
==About this Structure==
==About this Structure==
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[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
[[Category: Wwp1]]
[[Category: Wwp1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:23:14 2008''

Revision as of 22:23, 28 July 2008

Image:1nd7.png

Template:STRUCTURE 1nd7

Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase

Template:ABSTRACT PUBMED 12535537

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

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