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spinqualitylabelsall models PDB ID 1nd7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.1Å
Gene:	WWP1 (Homo sapiens)
Coordinates:	save as pdb, mmCIF, xml

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

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