3l3h: Difference between revisions
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<StructureSection load='3l3h' size='340' side='right'caption='[[3l3h]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3l3h' size='340' side='right'caption='[[3l3h]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3l3h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3l3h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/African_starling/England-Q/983/1979(H7N1)) Influenza A virus (A/African starling/England-Q/983/1979(H7N1))] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L3H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=3l3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3h OCA], [https://pdbe.org/3l3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3h RCSB], [https://www.ebi.ac.uk/pdbsum/3l3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3h 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=3l3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3h OCA], [https://pdbe.org/3l3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3h RCSB], [https://www.ebi.ac.uk/pdbsum/3l3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HA11_MOUSE HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
*[[MHC 3D structures|MHC 3D structures]] | *[[MHC 3D structures|MHC 3D structures]] | ||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Clements | [[Category: Clements CS]] | ||
[[Category: Dunstone | [[Category: Dunstone MA]] | ||
[[Category: Rossjohn | [[Category: Rossjohn J]] | ||
[[Category: Welland | [[Category: Welland A]] | ||
Revision as of 19:20, 1 November 2023
X-ray crystal structure of the F6A mutant of influenza A acid polymerase epitope PA224 bound to murine H2-Db MHCX-ray crystal structure of the F6A mutant of influenza A acid polymerase epitope PA224 bound to murine H2-Db MHC
Structural highlights
FunctionHA11_MOUSE Involved in the presentation of foreign antigens to the immune system. 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 PubMedResidues within processed protein fragments bound to major histocompatibility complex class I (MHC-I) glycoproteins have been considered to function as a series of "independent pegs" that either anchor the peptide (p) to the MHC-I and/or interact with the spectrum of alphabeta-T-cell receptors (TCRs) specific for the pMHC-I epitope in question. Mining of the extensive pMHC-I structural database established that many self- and viral peptides show extensive and direct interresidue interactions, an unexpected finding that has led us to the idea of "constrained" peptides. Mutational analysis of two constrained peptides (the HLA B44 restricted self-peptide (B44DPalpha-EEFGRAFSF) and an H2-D(b) restricted influenza peptide (D(b)PA, SSLENFRAYV) demonstrated that the conformation of the prominently exposed arginine in both peptides was governed by interactions with MHC-I-orientated flanking residues from the peptide itself. Using reverse genetics in a murine influenza model, we revealed that mutation of an MHC-I-orientated residue (SSLENFRAYV --> SSLENARAYV) within the constrained PA peptide resulted in a diminished cytotoxic T lymphocyte (CTL) response and the recruitment of a limited pMHC-I specific TCR repertoire. Interactions between individual peptide positions can thus impose fine control on the conformation of pMHC-I epitopes, whereas the perturbation of such constraints can lead to a previously unappreciated mechanism of viral escape. Constraints within major histocompatibility complex class I restricted peptides: presentation and consequences for T-cell recognition.,Theodossis A, Guillonneau C, Welland A, Ely LK, Clements CS, Williamson NA, Webb AI, Wilce JA, Mulder RJ, Dunstone MA, Doherty PC, McCluskey J, Purcell AW, Turner SJ, Rossjohn J Proc Natl Acad Sci U S A. 2010 Mar 23;107(12):5534-9. Epub 2010 Mar 8. PMID:20212169[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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