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EC Number
Crystallization (Commentary)
2.3.2.B8
determination of the crystal of a complex between the HECT domain NEDD4L and the E2 UbcH5B bearing a covantly-linked ubiquitin at its active site to gain insights of the ubiquitin transfer from an associated E2 to the acceptor cysteine in the HECT domain C-lobe. HECT contains is bilobed, consists of N-terminal N-lobe and C-terminal C-lobe. The C-lobe is essential for the E2-to-E3 ubiquitin transfer and the N-lobe is essential for the the further protein substrate processivity, the transfer of the ubiquitin from E3 to the substrate
2.3.2.B8
the WW domains proceeding the catalytic HECT domain play an inhibitory role by binding directly to HECT. The WW2 domain and a following linker allosterically lock HECT in an inactive state inhibiting E2-E3 transthiolation. Binding of the Ndfip1 adaptor or JNK1-mediated phosphorylation relieves the auto-inhibition of Itch in a WW2-dependent manner
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