The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity (Q27631051)

2

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A Brunmark

3

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N Mattsson

4

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M R Jackson

5

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P A Peterson

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L Teyton

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I A Wilson

MUC1 peptide epitopes associated with five different H‐2 class I molecules

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language of work or name

English

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publication date

March 2001

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published in

Immunity

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volume

14

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issue

3

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page(s)

231-42

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cites work

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Conformational differences in major histocompatibility complex-peptide complexes can result in alloreactivity.

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Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids

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Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical

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T cell receptor (TCR) recognition of MHC class I variants: intermolecular second-site reversion provides evidence for peptide/MHC conformational variation

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The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue

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