The solution structure of a class II major histocompatibility complex superantigen binding domain.
We have used 600 MHz 1H 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-Ab(beta)-(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-Ab(beta)-(60-90), which is mostly alpha-helical, is more similar to the corresponding region of the class II MHC protein HLA-DR1 than to the class I MHC protein HLA-A2. Arg-72 and Arg-80 lie on the same side of the helix and face away from the antigenic peptide binding groove. His-81, implicated in both superantigen and peptide binding, is located midway between the surface defined by Arg-72/Arg-80 and residues that define the inside of the peptide binding groove, allowing for its participation in both types of binding.
Jablonsky
M J
MJ
Comprehensive Cancer Care Center, Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 35294, USA.
Subramaniam
P S
PS
Johnson
H M
HM
Russell
J K
JK
Krishna
N R
NR
D000595:Amino Acid Sequence; D000818:Animals; D000949:Histocompatibility Antigens Class II / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure
D000949:Histocompatibility Antigens Class II