Classical and nonclassical class I major histocompatibility complex molecules exhibit subtle conformational differences that affect binding to CD8alphaalpha.
The cell surface molecules CD4 and CD8 greatly enhance the sensitivity of T-cell antigen recognition, acting as "co-receptors" by binding to the same major histocompatibility complex (MHC) molecules as the T-cell receptor (TCR). Here we use surface plasmon resonance to study the binding of...
Κύριοι συγγραφείς: | Gao, G, Willcox, B, Wyer, JR, Boulter, J, O'Callaghan, C, Maenaka, K, Stuart, D, Jones, E, Van Der Merwe, P, Bell, J, Jakobsen, B |
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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
2000
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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T cell receptor and coreceptor CD8 alphaalpha bind peptide-MHC independently and with distinct kinetics.
ανά: Wyer, JR, κ.ά.
Έκδοση: (1999) -
Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.
ανά: O'Callaghan, C, κ.ά.
Έκδοση: (1998) -
Production of soluble alphabeta T-cell receptor heterodimers suitable for biophysical analysis of ligand binding.
ανά: Willcox, B, κ.ά.
Έκδοση: (1999) -
BirA enzyme: production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation.
ανά: O'Callaghan, C, κ.ά.
Έκδοση: (1999) -
Engagement of a T cell receptor by major histocompatibility complex irrespective of peptide.
ανά: Vessey, S, κ.ά.
Έκδοση: (1997)