Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide

Chihiro Motozono; James A. Pearson; Evy De Leenheer; Pierre J. Rizkallah; Konrad Beck; Andrew Trimby; Andrew K. Sewell; F. Susan Wong; David K. Cole

doi:10.1074/jbc.M114.622522

Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide

Chihiro Motozono, James A. Pearson, Evy De Leenheer, Pierre J. Rizkallah, Konrad Beck, Andrew Trimby, Andrew K. Sewell, F. Susan Wong, David K. Cole

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

Abstract

Background: CD8⁺ T-cells play a central role in type 1 diabetes (T1D) by recognizing insulin peptides displayed by MHC. Results: A novel flexible MHC binding mode accommodates extra C-terminal peptide residues. Conclusion: Unusual peptide-MHC binding might explain weak TCR affinity of a natural T1D epitope. Significance: MHC peptide binding can be highly flexible around the F-binding pocket.

Original language	English
Pages (from-to)	18924-18933
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M114.622522
Publication status	Published - Jul 31 2015
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M114.622522

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title = "Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide",

abstract = "Background: CD8+ T-cells play a central role in type 1 diabetes (T1D) by recognizing insulin peptides displayed by MHC. Results: A novel flexible MHC binding mode accommodates extra C-terminal peptide residues. Conclusion: Unusual peptide-MHC binding might explain weak TCR affinity of a natural T1D epitope. Significance: MHC peptide binding can be highly flexible around the F-binding pocket.",

author = "Chihiro Motozono and Pearson, {James A.} and {De Leenheer}, Evy and Rizkallah, {Pierre J.} and Konrad Beck and Andrew Trimby and Sewell, {Andrew K.} and Wong, {F. Susan} and Cole, {David K.}",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

month = jul,

day = "31",

doi = "10.1074/jbc.M114.622522",

language = "English",

volume = "290",

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journal = "Journal of Biological Chemistry",

issn = "0021-9258",

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T1 - Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide

AU - Motozono, Chihiro

AU - Pearson, James A.

AU - De Leenheer, Evy

AU - Rizkallah, Pierre J.

AU - Beck, Konrad

AU - Trimby, Andrew

AU - Sewell, Andrew K.

AU - Wong, F. Susan

AU - Cole, David K.

PY - 2015/7/31

Y1 - 2015/7/31

N2 - Background: CD8+ T-cells play a central role in type 1 diabetes (T1D) by recognizing insulin peptides displayed by MHC. Results: A novel flexible MHC binding mode accommodates extra C-terminal peptide residues. Conclusion: Unusual peptide-MHC binding might explain weak TCR affinity of a natural T1D epitope. Significance: MHC peptide binding can be highly flexible around the F-binding pocket.

AB - Background: CD8+ T-cells play a central role in type 1 diabetes (T1D) by recognizing insulin peptides displayed by MHC. Results: A novel flexible MHC binding mode accommodates extra C-terminal peptide residues. Conclusion: Unusual peptide-MHC binding might explain weak TCR affinity of a natural T1D epitope. Significance: MHC peptide binding can be highly flexible around the F-binding pocket.

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SN - 0021-9258

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SP - 18924

EP - 18933

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 31

ER -

Distortion of the major histocompatibility complex class i binding groove to accommodate an insulin-derived 10-mer peptide

Abstract

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