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3pab

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Revision as of 22:48, 24 December 2014

Crystal Structure of H2-Kb in complex with a mutant of the chicken ovalbumin epitope OVA-E1

Structural highlights

3pab is a 6 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1vac, 3p9l, 3p9m
Gene:	H2-K1, H2-K (Mus musculus), B2m (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system. [OVAL_CHICK] Non-inhibitory serpin. Storage protein of egg white.^[1] ^[2] [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

Publication Abstract from PubMed

High-avidity interactions between TCRs and peptide + class I MHC (pMHCI) epitopes drive CTL activation and expansion. Intriguing questions remain concerning the constraints determining optimal TCR/pMHCI binding. The present analysis uses the TCR transgenic OT-I model to assess how varying profiles of TCR/pMHCI avidity influence naive CTL proliferation and the acquisition of effector function following exposure to the cognate H-2K(b)/OVA(257-264) (SIINFEKL) epitope and to mutants provided as peptide or in engineered influenza A viruses. Stimulating naive OT-I CD8(+) T cells in vitro with SIINFEKL induced full CTL proliferation and differentiation that was largely independent of any need for costimulation. By contrast, in vitro activation with the low-affinity EIINFEKL or SIIGFEKL ligands depended on the provision of IL-2 and other costimulatory signals. Importantly, although they did generate potent endogenous responses, infection of mice with influenza A viruses expressing these same OVA(257) variants failed to induce the activation of adoptively transferred naive OT-I CTLps, an effect that was only partially overcome by priming with a lipopeptide vaccine. Subsequent structural and biophysical analysis of H2-K(b)OVA(257), H2-K(b)E1, and H2-K(b)G4 established that these variations introduce small changes at the pMHCI interface and decrease epitope stability in ways that would likely impact cell surface presentation and recognition. Overall, it seems that there is an activation threshold for naive CTLps, that minimal alterations in peptide sequence can have profound effects, and that the antigenic requirements for the in vitro and in vivo induction of CTL proliferation and effector function differ substantially.

Affinity Thresholds for Naive CD8+ CTL Activation by Peptides and Engineered Influenza A Viruses.,Denton AE, Wesselingh R, Gras S, Guillonneau C, Olson MR, Mintern JD, Zeng W, Jackson DC, Rossjohn J, Hodgkin PD, Doherty PC, Turner SJ J Immunol. 2011 Oct 28. PMID:22039305^[3]

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

References

↑ Meek RL, Walsh KA, Palmiter RD. The signal sequence of ovalbumin is located near the NH2 terminus. J Biol Chem. 1982 Oct 25;257(20):12245-51. PMID:6749856
↑ Robinson A, Meredith C, Austen BM. Isolation and properties of the signal region from ovalbumin. FEBS Lett. 1986 Jul 28;203(2):243-6. PMID:3732511
↑ Denton AE, Wesselingh R, Gras S, Guillonneau C, Olson MR, Mintern JD, Zeng W, Jackson DC, Rossjohn J, Hodgkin PD, Doherty PC, Turner SJ. Affinity Thresholds for Naive CD8+ CTL Activation by Peptides and Engineered Influenza A Viruses. J Immunol. 2011 Oct 28. PMID:22039305 doi:10.4049/jimmunol.1003937

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3pab"

@@ Line 7: / Line 7: @@
 <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=3pab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pab RCSB], [http://www.ebi.ac.uk/pdbsum/3pab PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/OVAL_CHICK OVAL_CHICK]] Non-inhibitory serpin. Storage protein of egg white.<ref>PMID:6749856</ref> <ref>PMID:3732511</ref>  [[http://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3pab

From Proteopedia

Revision as of 22:48, 24 December 2014

Crystal Structure of H2-Kb in complex with a mutant of the chicken ovalbumin epitope OVA-E1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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