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Updated: Apr 1, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Structure of the HECT domain of human WWP2
Wei Gong1, Xiaodan Zhang1, Wen Zhang1
1Institutes of Biomedical Sciences and School of Basic Medical Sciences, Fudan University, People's Republic of China.
Abstract:
WWP2 is a HECT-domain ubiquitin ligase of the Nedd4 family, which is involved in various important biological processes, such as protein degradation, membrane-protein sorting and transportation, the immune response, pluripotency of embryonic stem cells, tumourigenesis and metastasis. The HECT domain provides the intrinsic ubiquitin ligase activity of WWP2. Here, the expression, purification, crystallization and crystallographic analysis of the HECT domain of human WWP2 (HECT(WWP2)) are reported. HECT(WWP2) has been crystallized and the crystals diffracted to 2.50 Å resolution. They belonged to space group P41212 and the structure has been solved via molecular replacement. The overall structure of HECT(WWP2) has an inverted T-shape. This structure displays a high degree of conservation with previously published structures of Nedd4 subfamily members.
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