PMID:15465811
| Citation |
Dodd, RB, Allen, MD, Brown, SE, Sanderson, CM, Duncan, LM, Lehner, PJ, Bycroft, M and Read, RJ (2004) Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain. J. Biol. Chem. 279:53840-7 |
|---|---|
| Abstract |
RING domains are found in a large number of eukaryotic proteins. Most function as E3 ubiquitin-protein ligases, catalyzing the terminal step in the ubiquitination process. Structurally, these domains have been characterized as binding two zinc ions in a stable cross-brace motif. The tumorigenic human gamma-herpesvirus Kaposi's sarcoma-associated herpesvirus encodes a ubiquitin-protein ligase termed K3, which functions as an immune evasion molecule by ubiquitinating major histocompatibility complex class I. K3 possesses at its N terminus a domain related to cellular RING domains but with an altered zinc ligand arrangement. This domain was initially characterized as a plant homeodomain, a structure not previously known to function as an E3. Here, it is conclusively demonstrated that the K3 N-terminal domain is a variant member of the RING domain family and not a plant homeodomain. The domain is found to interact with the cellular ubiquitin-conjugating enzymes UbcH5A to -C and UbcH13, which dock to the equivalent surface as on classical cellular RING domains. Interaction with UbcH13 suggests a possible role for K3 in catalyzing Lys(63)-linked ubiquitination. |
| Links |
PubMed Online version:10.1074/jbc.M409662200 |
| Keywords |
Amino Acid Sequence; Herpesvirus 8, Human/metabolism; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Static Electricity; Tryptophan/chemistry; Two-Hybrid System Techniques; Ubiquitin/chemistry; Viral Proteins/chemistry; Zinc/chemistry |
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