The Solution Structure of a Class II Major Histocompatibility Complex Superantigen Binding Domain
| Autor: | H.M. Johnson, Jablonsky Mj, Prem S. Subramaniam, Jeffry K. Russell, N.R. Krishna |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Molecular Structure biology Stereochemistry Molecular Sequence Data Histocompatibility Antigens Class II Biophysics chemical and pharmacologic phenomena Peptide binding Cell Biology Nuclear magnetic resonance spectroscopy Enterotoxin Major histocompatibility complex Biochemistry Mice Helix biology.protein Superantigen Animals Amino Acid Sequence Molecular Biology Two-dimensional nuclear magnetic resonance spectroscopy Binding domain |
| Zdroj: | Biochemical and Biophysical Research Communications. 234:660-665 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.6692 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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