Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding

Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding

Through major histocompatibility complex class Ia leader sequence-derived (VL9) peptide binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by HLA-E, a preference subsequently su...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Walters, L, Harlos, K, Brackenridge, S, Rozbesky, D, Barrett, J, Jain, V, Walter, T, O'Callaghan, C, Borrow, P, Toebes, M, Hansen, S, Sacha, J, Abdulhaqq, S, Greene, J, Früh, K, Marshall, E, Picker, L, Jones, E, McMichael, A, Gillespie, G
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	Springer Nature 2018

Παρόμοια τεκμήρια

Author Correction: Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding.
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Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
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Έκδοση: (2018-08-01)

Author Correction: Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
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