I got three binding sites when I run CD79b into peptiMap web-server (which identify/predict the binding sites on protein services). I have attached a table of the AA residues of each of the three sites obtained by PeptiMap.

I want to know (or even have some clues) which of these sites ( provided by peptimap) takes part in dimerzation of CD79a&b.

Some inputs that can help in concluding an answer to the above question are as follows:

1- A&B chains of CD79b together form a homodimer. On the other

hand, CD79b&a form a heterodimer

2- CD79b homodimerformed due to a disulfide bond between Cys

136 residue from its chain A& cys 136 of its chain B. Of course,

the two chains are of identical structure.

3- The dimerization between CD79a&b (the two subunits of CD79

protein) is also through a disulfide bond, and it is between Cys

113 from CD79a and residue cys 136 of CD79b.

A table with the AA residues of the three sites identified by PeptiMap is attached.

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