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Mine3leo

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1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
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Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
1
Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
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Dues of the RING domain (as well as the Zn++ ions) are required for proper foldingBinding Determinants of Rocsand function of the protein [7,9,15,16,17]. The importance to E3 ligase function of residues or domains outside of the RING domain is not currently understood. RING E3's can be further categorized as either single or multiprotein complexes. Single protein E3's, like c-Cbl, perform the enti
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Dues of the RING domain (as well as the Zn++ ions) are required for proper foldingBinding Determinants of Rocsand function of the protein [7,9,15,16,17]. The importance to E3 ligase function of residues or domains outside of the RING domain is not currently understood. RING E3's can be further categorized as either single or multiprotein complexes. Single protein E3's, like c-Cbl, perform the enti
1
For the Sry transgenic mice, R. Watkins (UCLA), R. Bijlani (UCLA), M. Cheng (UW), D. K. Nguyen (UW), N. Krakauer (UC Berkeley), and P. Mann (Tufts U) for technical and editorial assistance.Author ContributionsConceived and designed the experiments: CD JX. Performed the experiments: JX XD. Analyzed the data: CD JX XD. Wrote the paper: CD JX.Many aspects of cell and developmental biology requi
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Tion via a thiolester linkage to an internal cysteine in E1, which then transfers the ubiquitin to a cysteine residue of an E2 protein. The E2 interacts with an E3 to mediate covalent attachment of ubiquitin onto substrate proteins. Repeated rounds of E2/E3mediated ubiquitin transfer result in polyubiquitylation, allowing substrate proteins to be recognized and destroyed by the proteasome. Vertebr
1
Tion via a thiolester linkage to an internal cysteine in E1, which then transfers the ubiquitin to a cysteine residue of an E2 protein. The E2 interacts with an E3 to mediate covalent attachment of ubiquitin onto substrate proteins. Repeated rounds of E2/E3mediated ubiquitin transfer result in polyubiquitylation, allowing substrate proteins to be recognized and destroyed by the proteasome. Vertebr