1vyx

From Proteopedia

(Difference between revisions)

Revision as of 08:16, 10 November 2021

Solution structure of the KSHV K3 N-terminal domain

Structural highlights

1vyx is a 1 chain structure with sequence from Hhv-8. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1chc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MIR1_HHV8P] E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes. Binds target molecules through transmembrane interaction. E3 ubiquitin-protein ligases accept ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfer it to target protein. The result of this ubiquitination is the enhancement of the endocytosis of the target chain and the delivery to the lysosome, where it is proteolytically destroyed. Induces ubiquitination not only on lysines, but also on cysteine residues.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ishido S, Wang C, Lee BS, Cohen GB, Jung JU. Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins. J Virol. 2000 Jun;74(11):5300-9. PMID:10799607
↑ Coscoy L, Ganem D. Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):8051-6. PMID:10859362 doi:http://dx.doi.org/10.1073/pnas.140129797
↑ Coscoy L, Sanchez DJ, Ganem D. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol. 2001 Dec 24;155(7):1265-73. Epub 2001 Dec 24. PMID:11756476 doi:http://dx.doi.org/10.1083/jcb.200111010
↑ Sanchez DJ, Gumperz JE, Ganem D. Regulation of CD1d expression and function by a herpesvirus infection. J Clin Invest. 2005 May;115(5):1369-78. PMID:15864354 doi:http://dx.doi.org/10.1172/JCI24041
↑ Cadwell K, Coscoy L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science. 2005 Jul 1;309(5731):127-30. PMID:15994556 doi:http://dx.doi.org/10.1126/science.1110340
↑ Dodd RB, Allen MD, Brown SE, Sanderson CM, Duncan LM, Lehner PJ, Bycroft M, Read RJ. Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain. J Biol Chem. 2004 Dec 17;279(51):53840-7. Epub 2004 Sep 30. PMID:15465811 doi:http://dx.doi.org/10.1074/jbc.M409662200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vyx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1vyx' size='340' side='right'caption='[[1vyx]], [[NMR_Ensembles_of_Models | 28 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-8 Hhv-8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VYX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hhv-8 Hhv-8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1chc|1chc]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1chc|1chc]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1vyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vyx RCSB], [http://www.ebi.ac.uk/pdbsum/1vyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyx ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyx OCA], [https://pdbe.org/1vyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vyx RCSB], [https://www.ebi.ac.uk/pdbsum/1vyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MIR1_HHV8P MIR1_HHV8P]] E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes. Binds target molecules through transmembrane interaction. E3 ubiquitin-protein ligases accept ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfer it to target protein. The result of this ubiquitination is the enhancement of the endocytosis of the target chain and the delivery to the lysosome, where it is proteolytically destroyed. Induces ubiquitination not only on lysines, but also on cysteine residues.<ref>PMID:10799607</ref> <ref>PMID:10859362</ref> <ref>PMID:11756476</ref> <ref>PMID:15864354</ref> <ref>PMID:15994556</ref>
+[[https://www.uniprot.org/uniprot/MIR1_HHV8P MIR1_HHV8P]] E3 ubiquitin-protein ligase which promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, presumably to prevent lysis of infected cells by cytotoxic T-lymphocytes. Binds target molecules through transmembrane interaction. E3 ubiquitin-protein ligases accept ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfer it to target protein. The result of this ubiquitination is the enhancement of the endocytosis of the target chain and the delivery to the lysosome, where it is proteolytically destroyed. Induces ubiquitination not only on lysines, but also on cysteine residues.<ref>PMID:10799607</ref> <ref>PMID:10859362</ref> <ref>PMID:11756476</ref> <ref>PMID:15864354</ref> <ref>PMID:15994556</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1vyx

From Proteopedia

Revision as of 08:16, 10 November 2021

Solution structure of the KSHV K3 N-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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