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- W1891789905 abstract "Abstract The RING domain is a cysteine‐rich sequence motif that can bind two zinc atoms. In the canonical RING motif, also called the C3HC4 motif, one zinc ion is bound to four cysteines, and the other ion to three cysteines and a histidine. The tetrahedral coordination is atypical and referred to as a ‘cross‐brace’ motif. There are now more than 380 RING motifs identified in the human genome. The RING domain has been shown to mediate a crucial step in the ubiquitination pathway that targets protein substrates for degradation by the 26 S proteasome. This pathway involves three enzymes, and the RING finger proteins have been classified in this scheme as ubiquitin ligases. There are actually nine structures of RING domains solved by X‐ray and NMR. The βαβ fold of the RING domain is conserved among all structures. The structures of RING domains in complex with other proteins involved in the ubiquitination pathway provide considerable insight into the molecular basis of ubiquitination. Recently, ubiquitination has been shown to be not only a simple protein removal system but also an indispensable regulatory process. This is underscored by the observation that many diseases, such as cancer and Parkinson's disease, are due to mutations in RING domains that prevent an efficient ubiquitination and degradation process. In this review, we compare the different structures of RING domains, analyze their functional aspects through structural information of RING domains in complex with other proteins, and describe medical aspects of RING finger proteins involved in cancer and Parkinson's disease." @default.
- W1891789905 created "2016-06-24" @default.
- W1891789905 creator A5035567220 @default.
- W1891789905 creator A5052112949 @default.
- W1891789905 creator A5075671745 @default.
- W1891789905 date "2004-03-05" @default.
- W1891789905 modified "2023-10-02" @default.
- W1891789905 title "RING Domain Proteins" @default.
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- W1891789905 doi "https://doi.org/10.1002/9781119951438.eibc0488" @default.
- W1891789905 hasPublicationYear "2004" @default.
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