1vyx: Difference between revisions
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[[Image:1vyx.gif|left|200px]] | [[Image:1vyx.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN''' | {{Structure | ||
|PDB= 1vyx |SIZE=350|CAPTION= <scene name='initialview01'>1vyx</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VYX is a [ | 1VYX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15465811 15465811] | ||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-binding protein]] | [[Category: zinc-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:49:57 2008'' | ||
Revision as of 15:49, 20 March 2008
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SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN
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. 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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