| Autor: |
Dessen A; Laboratory of Molecular Medicine, The Children's Hospital, Boston, Massachusetts 02115, USA. dessen@xtal22.tch.harvard.edu, Lawrence CM, Cupo S, Zaller DM, Wiley DC |
| Jazyk: |
angličtina |
| Zdroj: |
Immunity [Immunity] 1997 Oct; Vol. 7 (4), pp. 473-81. |
| DOI: |
10.1016/s1074-7613(00)80369-6 |
| Abstrakt: |
Genetic predisposition to rheumatoid arthritis (RA) is linked to the MHC class II allele HLA-DR4. The charge of the amino acid at DRbeta71 in the peptide-binding site appears to be critical in discriminating DR molecules linked to increased disease susceptibility. We have determined the 2.5 A x-ray structure of the DR4 molecule with the strongest linkage to RA (DRB1*0401) complexed with a human collagen II peptide. Details of a predicted salt bridge between lysine DRbeta71 and aspartic acid at the P4 peptide position suggest how it may participate in both antigen binding and TCR activation. A model is proposed for the DR4 recognition of collagen II (261-273), an antigen immunodominant in human-transgenic mouse models of RA. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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