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1vyx
From Proteopedia
(New page: 200px<br /><applet load="1vyx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vyx" /> '''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL...) |
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| - | [[Image:1vyx.gif|left|200px]]<br /><applet load="1vyx" size=" | + | [[Image:1vyx.gif|left|200px]]<br /><applet load="1vyx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vyx" /> | caption="1vyx" /> | ||
'''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN'''<br /> | '''SOLUTION STRUCTURE OF THE KSHV K3 N-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | RING domains are found in a large number of eukaryotic proteins. Most | + | 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== | ==About this Structure== | ||
| - | 1VYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1VYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allen, M | + | [[Category: Allen, M D.]] |
| - | [[Category: Brown, S | + | [[Category: Brown, S E.]] |
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
| - | [[Category: Dodd, R | + | [[Category: Dodd, R B.]] |
| - | [[Category: Duncan, L | + | [[Category: Duncan, L M.]] |
| - | [[Category: Lehner, P | + | [[Category: Lehner, P J.]] |
| - | [[Category: Read, R | + | [[Category: Read, R J.]] |
| - | [[Category: Sanderson, C | + | [[Category: Sanderson, C M.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: cross-brace motif]] | [[Category: cross-brace motif]] | ||
| Line 26: | Line 26: | ||
[[Category: zinc-binding protein]] | [[Category: zinc-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:45 2008'' |
Revision as of 13:38, 21 February 2008
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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 4 with as ligand. 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
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