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| - | {{Seed}} | |
| - | [[Image:1qlo.png|left|200px]] | |
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| - | <!-- | + | ==Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy== |
| - | The line below this paragraph, containing "STRUCTURE_1qlo", creates the "Structure Box" on the page.
| + | <StructureSection load='1qlo' size='340' side='right'caption='[[1qlo]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1qlo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QLO FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlo OCA], [https://pdbe.org/1qlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qlo RCSB], [https://www.ebi.ac.uk/pdbsum/1qlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qlo ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1qlo| PDB=1qlo | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ICP47_HHV11 ICP47_HHV11] Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.<ref>PMID:11254939</ref> <ref>PMID:7760936</ref> <ref>PMID:8187174</ref> <ref>PMID:8670825</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | ICP47 encoded by herpes simplex virus (HSV) is a key factor in the evasion of cellular immune response against HSV-infected cells. By specific inhibition of the transporter associated with antigen processing (TAP), ICP47 prevents peptide transport into the endoplasmic reticulum and subsequent loading of major histocompatibility complex (MHC) class I molecules. Amino acid residues 3-34 have been identified as the active domain. This domain appeared to be unstructured in aqueous solution, whereas after binding to membranes an alpha-helical conformation was observed. Here, we have analyzed the structure of ICP47(2-34) in a lipidlike environment by nuclear magnetic resonance (NMR) spectroscopy. In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32. Arg-16 is found on the C-terminus of the first helix, and Gly-33 serves as a terminator of the second helix. A loop between residues 17 and 21 is also evident in the structure. The relative orientation of the helices toward each other, however, could not be determined due to the paucity of NOEs from residues 18-21. |
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| - | ===STRUCTURE OF THE ACTIVE DOMAIN OF THE HERPES SIMPLEX VIRUS PROTEIN ICP47 IN WATER/SODIUM DODECYL SULFATE SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY===
| + | Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy.,Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:10521276<ref>PMID:10521276</ref> |
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| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_10521276}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 1qlo" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 10521276 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_10521276}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Human alphaherpesvirus 1 strain 17]] |
| - | 1QLO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLO OCA].
| + | [[Category: Large Structures]] |
| - | | + | [[Category: Holak TA]] |
| - | ==Reference== | + | [[Category: Neumann L]] |
| - | Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy., Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R, Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10521276 10521276]
| + | [[Category: Pfaender R]] |
| - | [[Category: Human herpesvirus 1]] | + | [[Category: Seger C]] |
| - | [[Category: Single protein]] | + | [[Category: Tampe R]] |
| - | [[Category: Holak, T A.]] | + | [[Category: Zweckstetter M]] |
| - | [[Category: Neumann, L.]] | + | |
| - | [[Category: Pfaender, R.]] | + | |
| - | [[Category: Seger, C.]] | + | |
| - | [[Category: Tampe, R.]] | + | |
| - | [[Category: Zweckstetter, M.]] | + | |
| - | [[Category: Herpes simplex virus]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Protein icp47]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:28:30 2008''
| + | |
| Structural highlights
Function
ICP47_HHV11 Plays a role in the inhibition of host immune response. Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules. Empty MHC I molecules are retained in the endoplasmic reticulum and ultimately directed to proteasomal degradation. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.[1] [2] [3] [4]
Publication Abstract from PubMed
ICP47 encoded by herpes simplex virus (HSV) is a key factor in the evasion of cellular immune response against HSV-infected cells. By specific inhibition of the transporter associated with antigen processing (TAP), ICP47 prevents peptide transport into the endoplasmic reticulum and subsequent loading of major histocompatibility complex (MHC) class I molecules. Amino acid residues 3-34 have been identified as the active domain. This domain appeared to be unstructured in aqueous solution, whereas after binding to membranes an alpha-helical conformation was observed. Here, we have analyzed the structure of ICP47(2-34) in a lipidlike environment by nuclear magnetic resonance (NMR) spectroscopy. In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32. Arg-16 is found on the C-terminus of the first helix, and Gly-33 serves as a terminator of the second helix. A loop between residues 17 and 21 is also evident in the structure. The relative orientation of the helices toward each other, however, could not be determined due to the paucity of NOEs from residues 18-21.
Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy.,Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:10521276[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Easterfield AJ, Austen BM, Westwood OM. Inhibition of antigen transport by expression of infected cell peptide 47 (ICP47) prevents cell surface expression of HLA in choriocarcinoma cell lines. J Reprod Immunol. 2001 Apr;50(1):19-40. PMID:11254939
- ↑ Fruh K, Ahn K, Djaballah H, Sempe P, van Endert PM, Tampe R, Peterson PA, Yang Y. A viral inhibitor of peptide transporters for antigen presentation. Nature. 1995 Jun 1;375(6530):415-8. PMID:7760936 doi:http://dx.doi.org/10.1038/375415a0
- ↑ York IA, Roop C, Andrews DW, Riddell SR, Graham FL, Johnson DC. A cytosolic herpes simplex virus protein inhibits antigen presentation to CD8+ T lymphocytes. Cell. 1994 May 20;77(4):525-35. PMID:8187174
- ↑ Ahn K, Meyer TH, Uebel S, Sempe P, Djaballah H, Yang Y, Peterson PA, Fruh K, Tampe R. Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47. EMBO J. 1996 Jul 1;15(13):3247-55. PMID:8670825
- ↑ Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R. Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:10521276
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