1vyx
From Proteopedia
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'''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN''' | '''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN''' | ||
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[[Category: Read, R J.]] | [[Category: Read, R J.]] | ||
[[Category: Sanderson, C M.]] | [[Category: Sanderson, C M.]] | ||
| - | [[Category: | + | [[Category: Cross-brace motif]] |
| - | [[Category: | + | [[Category: Ring domain]] |
| - | [[Category: | + | [[Category: Zinc-binding protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:55:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:56, 3 May 2008
SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN
Overview
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 Structure
1VYX is a Single protein structure of sequence from Human herpesvirus 8. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 12:55:58 2008
