1vyx
SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN
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OverviewOverview
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.
About this StructureAbout this Structure
1VYX is a Single protein structure of sequence from Human herpesvirus 4 with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain., Dodd RB, Allen MD, Brown SE, Sanderson CM, Duncan LM, Lehner PJ, Bycroft M, Read RJ, J Biol Chem. 2004 Dec 17;279(51):53840-7. Epub 2004 Sep 30. PMID:15465811
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