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Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Proceedings of the National Academy of Sciences, 108, 2011, 48, S. 19329-19334 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. |
|---|---|
| author |
Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. |
| spellingShingle |
Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. Proceedings of the National Academy of Sciences Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange Multidisciplinary |
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painter, corrie a. |
| spelling |
Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1108074108 <jats:p>HLA-DM is required for efficient peptide exchange on class II MHC molecules, but its mechanism of action is controversial. We trapped an intermediate state of class II MHC HLA-DR1 by substitution of αF54, resulting in a protein with increased HLA-DM binding affinity, weakened MHC-peptide hydrogen bonding as measured by hydrogen-deuterium exchange mass spectrometry, and increased susceptibility to DM-mediated peptide exchange. Structural analysis revealed a set of concerted conformational alterations at the N-terminal end of the peptide-binding site. These results suggest that interaction with HLA-DM is driven by a conformational change of the MHC II protein in the region of the α-subunit 3<jats:sub>10</jats:sub>helix and adjacent extended strand region, and provide a model for the mechanism of DM-mediated peptide exchange.</jats:p> Conformational lability in the class II MHC 3<sub>10</sub>helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange Proceedings of the National Academy of Sciences |
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| title |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_unstemmed |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_full |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_fullStr |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_full_unstemmed |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_short |
Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_sort |
conformational lability in the class ii mhc 3<sub>10</sub>helix and adjacent extended strand dictate hla-dm susceptibility and peptide exchange |
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Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1108074108 |
| publishDate |
2011 |
| physical |
19329-19334 |
| description |
<jats:p>HLA-DM is required for efficient peptide exchange on class II MHC molecules, but its mechanism of action is controversial. We trapped an intermediate state of class II MHC HLA-DR1 by substitution of αF54, resulting in a protein with increased HLA-DM binding affinity, weakened MHC-peptide hydrogen bonding as measured by hydrogen-deuterium exchange mass spectrometry, and increased susceptibility to DM-mediated peptide exchange. Structural analysis revealed a set of concerted conformational alterations at the N-terminal end of the peptide-binding site. These results suggest that interaction with HLA-DM is driven by a conformational change of the MHC II protein in the region of the α-subunit 3<jats:sub>10</jats:sub>helix and adjacent extended strand region, and provide a model for the mechanism of DM-mediated peptide exchange.</jats:p> |
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| author | Painter, Corrie A., Negroni, Maria P., Kellersberger, Katherine A., Zavala-Ruiz, Zarixia, Evans, James E., Stern, Lawrence J. |
| author_facet | Painter, Corrie A., Negroni, Maria P., Kellersberger, Katherine A., Zavala-Ruiz, Zarixia, Evans, James E., Stern, Lawrence J., Painter, Corrie A., Negroni, Maria P., Kellersberger, Katherine A., Zavala-Ruiz, Zarixia, Evans, James E., Stern, Lawrence J. |
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| description | <jats:p>HLA-DM is required for efficient peptide exchange on class II MHC molecules, but its mechanism of action is controversial. We trapped an intermediate state of class II MHC HLA-DR1 by substitution of αF54, resulting in a protein with increased HLA-DM binding affinity, weakened MHC-peptide hydrogen bonding as measured by hydrogen-deuterium exchange mass spectrometry, and increased susceptibility to DM-mediated peptide exchange. Structural analysis revealed a set of concerted conformational alterations at the N-terminal end of the peptide-binding site. These results suggest that interaction with HLA-DM is driven by a conformational change of the MHC II protein in the region of the α-subunit 3<jats:sub>10</jats:sub>helix and adjacent extended strand region, and provide a model for the mechanism of DM-mediated peptide exchange.</jats:p> |
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| imprint_str_mv | Proceedings of the National Academy of Sciences, 2011 |
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| spelling | Painter, Corrie A. Negroni, Maria P. Kellersberger, Katherine A. Zavala-Ruiz, Zarixia Evans, James E. Stern, Lawrence J. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1108074108 <jats:p>HLA-DM is required for efficient peptide exchange on class II MHC molecules, but its mechanism of action is controversial. We trapped an intermediate state of class II MHC HLA-DR1 by substitution of αF54, resulting in a protein with increased HLA-DM binding affinity, weakened MHC-peptide hydrogen bonding as measured by hydrogen-deuterium exchange mass spectrometry, and increased susceptibility to DM-mediated peptide exchange. Structural analysis revealed a set of concerted conformational alterations at the N-terminal end of the peptide-binding site. These results suggest that interaction with HLA-DM is driven by a conformational change of the MHC II protein in the region of the α-subunit 3<jats:sub>10</jats:sub>helix and adjacent extended strand region, and provide a model for the mechanism of DM-mediated peptide exchange.</jats:p> Conformational lability in the class II MHC 3<sub>10</sub>helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange Proceedings of the National Academy of Sciences |
| spellingShingle | Painter, Corrie A., Negroni, Maria P., Kellersberger, Katherine A., Zavala-Ruiz, Zarixia, Evans, James E., Stern, Lawrence J., Proceedings of the National Academy of Sciences, Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange, Multidisciplinary |
| title | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_full | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_fullStr | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_full_unstemmed | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_short | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| title_sort | conformational lability in the class ii mhc 3<sub>10</sub>helix and adjacent extended strand dictate hla-dm susceptibility and peptide exchange |
| title_unstemmed | Conformational lability in the class II MHC 310helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1108074108 |