View source for 4pgb


==MHC Class I in complex with modified Sendai virus nucleoprotein peptide FAPGNWPAL==
<StructureSection load='4pgb' size='340' side='right'caption='[[4pgb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pgb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Respirovirus_muris Respirovirus muris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=4pgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgb OCA], [https://pdbe.org/4pgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pgb RCSB], [https://www.ebi.ac.uk/pdbsum/4pgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MHC class I molecules present a variable but limited repertoire of antigenic peptides for T-cell recognition. Understanding how peptide selection is achieved requires mechanistic insights into the interactions between the MHC I and candidate peptides. We find that, at first encounter, MHC I H-2K(b) considers a wide range of peptides, including those with expanded N termini and unfitting anchor residues. Discrimination occurs in the second step, when noncanonical peptides dissociate with faster exchange rates. This second step exhibits remarkable temperature sensitivity, as illustrated by numerous noncanonical peptides presented by H-2K(b) in cells cultured at 26 degrees C relative to 37 degrees C. Crystallographic analyses of H-2K(b)-peptide complexes suggest that a conformational adaptation of H-2K(b) drives the decisive step in peptide selection. We propose that MHC class I molecules consider initially a large peptide pool, subsequently refined by a temperature-sensitive induced-fit mechanism to retain the canonical peptide repertoire.

The first step of peptide selection in antigen presentation by MHC class I molecules.,Garstka MA, Fish A, Celie PH, Joosten RP, Janssen GM, Berlin I, Hoppes R, Stadnik M, Janssen L, Ovaa H, van Veelen PA, Perrakis A, Neefjes J Proc Natl Acad Sci U S A. 2015 Feb 3;112(5):1505-10. doi:, 10.1073/pnas.1416543112. Epub 2015 Jan 20. PMID:25605945<ref>PMID:25605945</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pgb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Respirovirus muris]]
[[Category: Celie PHN]]
[[Category: Joosten RP]]
[[Category: Neefjes J]]
[[Category: Perrakis A]]