1vyx: Difference between revisions

Revision as of 16:41, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vyx.png

Template:STRUCTURE 1vyx

SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAINSOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN

Template:ABSTRACT PUBMED 15465811

About this StructureAbout this Structure

1VYX is a Single protein structure of sequence from Human herpesvirus 8. Full experimental 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15465811}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15465811 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15465811}}
 ==About this Structure==
-VYX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA].
+VYX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA].
 ==Reference==
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 [[Category: Ring domain]]
 [[Category: Zinc-binding protein]]
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