1vyx: Difference between revisions

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[[Image:1vyx.gif|left|200px]]
[[Image:1vyx.gif|left|200px]]


{{Structure
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{{STRUCTURE_1vyx| PDB=1vyx  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyx OCA], [http://www.ebi.ac.uk/pdbsum/1vyx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vyx RCSB]</span>
}}


'''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: cross-brace motif]]
[[Category: Cross-brace motif]]
[[Category: ring domain]]
[[Category: Ring domain]]
[[Category: zinc-binding protein]]
[[Category: Zinc-binding protein]]
 
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Revision as of 12:56, 3 May 2008

File:1vyx.gif

Template:STRUCTURE 1vyx

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 8. 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 Page seeded by OCA on Sat May 3 12:55:58 2008

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