4Y07

Crystal structure of the HECT domain of human WWP2

Summary for 4Y07

• Entry DOI: 10.2210/pdb4y07/pdb
• Descriptor: NEDD4-like E3 ubiquitin-protein ligase WWP2 (2 entities in total)
• Functional Keywords: e3 ligase, hect domain, ligase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : O00308
• Total number of polymer chains: 1
• Total formula weight: 44771.23

Authors

Gong, W.,Li, J.,Li, Z.,Xu, Y. (deposition date: 2015-02-05, release date: 2015-11-04, Last modification date: 2023-11-08)

Primary citation

Gong, W.,Zhang, X.,Zhang, W.,Li, J.,Li, Z.
Structure of the HECT domain of human WWP2
Acta Crystallogr.,Sect.F, 71:1251-1257, 2015

PubMed 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.

PubMed: 26457515
DOI: 10.1107/S2053230X1501554X

Experimental method

X-RAY DIFFRACTION (2.507 Å)