The solution structure of a class II major histocompatibility complex superantigen binding domain
MJ Jablonsky, PS Subramaniam, HM Johnson… - Biochemical and …, 1997 - Elsevier
We have used 600 MHz1H NMR spectroscopy data to determine the solution structure of a
31-residue domain of a murine class II major histocompatibility (MHC) protein. This domain, I-
Aβb-(60-90), binds to the superantigen staphylococcal enterotoxin A. Distance geometry
and dynamical simulated annealing calculations were performed using NOESY-and COSY-
deduced constraints. I-Aβb-(60-90), which is mostly α-helical, is more similar to the
corresponding region of the class II MHC protein HLA-DR1 than to the class I MHC protein …
31-residue domain of a murine class II major histocompatibility (MHC) protein. This domain, I-
Aβb-(60-90), binds to the superantigen staphylococcal enterotoxin A. Distance geometry
and dynamical simulated annealing calculations were performed using NOESY-and COSY-
deduced constraints. I-Aβb-(60-90), which is mostly α-helical, is more similar to the
corresponding region of the class II MHC protein HLA-DR1 than to the class I MHC protein …
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