WWP2: Difference between revisions
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The thioester bond formation between an active site Cystine on HECT E3 Ligases and the ubiquitin ligand differentiates the HECT family of enzymes from the more abundant RING ('''R'''eally '''I'''nteresting '''N'''ew '''G'''ene) family of ubiquitin ligases which mediate ubiquitin transfer through non-covalent interactions. Within HECT E3 Ligases, WWP2 falls into the NEDD 4 family (named after the instance in which the first member was discovered: a study of developmentally down-regulated proteins in neuronal embryonic mouse cells) which generally target proteins with a PPxY motif. NEDD4 E3 Ligases consist of an amino-terminal C2 domain, between two and four WW domains, and a carboxy-terminal HECT domain. Two conformational states (a ground state inverse T shape and catalytically active L shape) have been observed. | The thioester bond formation between an active site Cystine on HECT E3 Ligases and the ubiquitin ligand differentiates the HECT family of enzymes from the more abundant RING ('''R'''eally '''I'''nteresting '''N'''ew '''G'''ene) family of ubiquitin ligases which mediate ubiquitin transfer through non-covalent interactions. Within HECT E3 Ligases, WWP2 falls into the NEDD 4 family (named after the instance in which the first member was discovered: a study of developmentally down-regulated proteins in neuronal embryonic mouse cells) which generally target proteins with a PPxY motif. NEDD4 E3 Ligases consist of an amino-terminal C2 domain, between two and four WW domains, and a carboxy-terminal HECT domain. Two conformational states (a ground state inverse T shape and catalytically active L shape) have been observed. | ||
See [[Ubiquitin protein ligase]]. | |||
==Structure== | ==Structure== | ||
