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| | <StructureSection load='4zfz' size='340' side='right'caption='[[4zfz]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='4zfz' size='340' side='right'caption='[[4zfz]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zfz]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Macmu Macmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZFZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zfz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_mulatta Macaca mulatta] and [https://en.wikipedia.org/wiki/Simian_immunodeficiency_virus_(F236/SMH4_ISOLATE)_(SOOTY_MANGABEY) Simian immunodeficiency virus (F236/SMH4 ISOLATE) (SOOTY MANGABEY)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZFZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9544 MACMU])</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=4zfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zfz OCA], [https://pdbe.org/4zfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zfz RCSB], [https://www.ebi.ac.uk/pdbsum/4zfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zfz ProSAT]</span></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=4zfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zfz OCA], [http://pdbe.org/4zfz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zfz RCSB], [http://www.ebi.ac.uk/pdbsum/4zfz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zfz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NEF_SIVS4 NEF_SIVS4]] Seems to play a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Enhances virus infectivity and pathogenicity. Probably involved in viral immune evasion mechanisms (By similarity). In infected CD4(+) T-lymphocytes, down-regulates cell surface expression of CD4, CD28, CD3, and MHC-I or MHC-II molecules.<ref>PMID:16051847</ref> Interferes with TCR signaling from the cell membrane. Interacts with CD247/TCRZ (TCR zeta chain) and exert potent down-regulation of cell surface TCR/CD3 complexes.<ref>PMID:16051847</ref> [[http://www.uniprot.org/uniprot/B2MG_MACMU B2MG_MACMU]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system (By similarity). | + | [https://www.uniprot.org/uniprot/K4MU32_MACMU K4MU32_MACMU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
| - | *[[MHC 3D structures of MHC|MHC 3D structures of MHC]] | + | *[[MHC 3D structures|MHC 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Macmu]] | + | [[Category: Macaca mulatta]] |
| - | [[Category: Morita, D]] | + | [[Category: Morita D]] |
| - | [[Category: Sugita, M]] | + | [[Category: Sugita M]] |
| - | [[Category: Aid]]
| + | |
| - | [[Category: Antigen presentation]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Lipopeptide]]
| + | |
| - | [[Category: Mhc]]
| + | |
| Structural highlights
Function
K4MU32_MACMU
Publication Abstract from PubMed
The covalent conjugation of a 14-carbon saturated fatty acid (myristic acid) to the amino-terminal glycine residue is critical for some viral proteins to function. This protein lipidation modification, termed N-myristoylation, is targeted by host cytotoxic T lymphocytes (CTLs) that specifically recognize N-myristoylated short peptides; however, the molecular mechanisms underlying lipopeptide antigen (Ag) presentation remain elusive. Here we show that a primate major histocompatibility complex (MHC) class I-encoded protein is capable of binding N-myristoylated 5-mer peptides and presenting them to specific CTLs. A high-resolution X-ray crystallographic analysis of the MHC class I:lipopeptide complex reveals an Ag-binding groove that is elaborately constructed to bind N-myristoylated short peptides rather than prototypic 9-mer peptides. The identification of lipopeptide-specific, MHC class I-restricted CTLs indicates that the widely accepted concept of MHC class I-mediated presentation of long peptides to CTLs may need some modifications to incorporate a novel MHC class I function of lipopeptide Ag presentation.
Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex.,Morita D, Yamamoto Y, Mizutani T, Ishikawa T, Suzuki J, Igarashi T, Mori N, Shiina T, Inoko H, Fujita H, Iwai K, Tanaka Y, Mikami B, Sugita M Nat Commun. 2016 Jan 13;7:10356. doi: 10.1038/ncomms10356. PMID:26758274[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morita D, Yamamoto Y, Mizutani T, Ishikawa T, Suzuki J, Igarashi T, Mori N, Shiina T, Inoko H, Fujita H, Iwai K, Tanaka Y, Mikami B, Sugita M. Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex. Nat Commun. 2016 Jan 13;7:10356. doi: 10.1038/ncomms10356. PMID:26758274 doi:http://dx.doi.org/10.1038/ncomms10356
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