Role of phosphorylation in conformational adaptability of bovine myelin basic protein

1990 ◽  
Vol 7 (1) ◽  
pp. 32-40 ◽  
Author(s):  
Gladys E. Deibler ◽  
Audrey L. Stone ◽  
Marian W. Kies



2012 ◽  
Vol 189 (6) ◽  
pp. 2897-2908 ◽  
Author(s):  
Jacqueline A. Quandt ◽  
Jaebong Huh ◽  
Mirza Baig ◽  
Karen Yao ◽  
Naoko Ito ◽  
...  


2002 ◽  
Vol 249 (11) ◽  
pp. 1552-1555 ◽  
Author(s):  
Eleonora Cocco ◽  
Cristina Mancosu ◽  
Elisabetta Fadda ◽  
Maria Rita Murru ◽  
Gianna Costa ◽  
...  




2002 ◽  
Vol 18 (4) ◽  
pp. 259-270 ◽  
Author(s):  
Maria Manczak ◽  
Shuguang Jiang ◽  
Beata Orzechowska ◽  
Grazyna Adamus


1989 ◽  
Vol 169 (6) ◽  
pp. 2239-2244 ◽  
Author(s):  
C B Davis ◽  
J M Buerstedde ◽  
D J McKean ◽  
P P Jones ◽  
H O McDevitt ◽  
...  

Proteins encoded by genes in the MHC are highly polymorphic. For class II proteins the highest level of polymorphism is found in distinct regions of variability, notably in the membrane-distal domains. To investigate the role of such residues in antigen presentation, we have tested cells transfected with wild-type or mutant I-Ak beta chains for their ability to present the NH2-terminal peptide of myelin basic protein to a panel of T cell clones. We were unable to detect a gross effect on peptide binding, in that all of the mutant cell lines presented antigen to at least one of the cloned T cells. However, the results imply that the more NH2-terminal residues, particularly 12 and 14, are involved in peptide interactions. Mutations at these residues presented antigen only at high antigen concentrations. Furthermore, residues of the more COOH-terminal regions appear to determine TCR interactions. Mutations in the predicted alpha-helical regions of the beta chain affected antigen presentation without abolishing peptide binding.





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