In article <1staff.dental.2.000E0AEE at muwaye.unimelb.edu.au>,
<1staff.dental at muwaye.unimelb.edu.au> wrote:
>I am looking for the binding site for C1q on the Cgamma2 domain on IgG.
>Would anyone out there in the newsworld be able to provide me with a guide.
>Even a handy reference would be greatly appreciated.
>>>Look forward to some juicy correspondence.
>Cheers
>>>>Chris Sotiropoulos
>>E.mail :::: chris=sotiropoulos%dental at muwaye.unimelb.EDU.AU
It's a complex issue but I suggest that you look at the following
Structural motifs involved in human IgG antibody effector functions
J. Greenwood, M. Clark, H. Waldmann Eur. J. Immunol. 1993 23, 1098-1104
Effector functions of matched sets of recombinant human IgG subclass
antibodies. J. Greenwood, M. Clark in Protein engineering of antibody
molecules for prophylactic and therapeutic applications in man
Pub. Academic Titles, Nottingham UK 85-100 1994
(also other chapters by S. Morrison and by R. Jefferis in the same volume)
In mouse the sequence Glu Tyr Lys Cys Lys 318-322 was identified by
Duncan and Winter. However this does not account for the difference in human
as all IgGs have identical sequence here. We and others have identified
multiple residues which alter affinity for C1q.
I don't think that anyone can give a definitive answer yet as to the absolute
binding site but we can identify residues which are responsible for the
observed differences in effector functions between species and isotypes.
Hope this helps.
o/ \\ // || ,_ o Mike Clark, mrc7 at cus.cam.ac.uk
<\__,\\ // __o || / /\, Cambridge University, Dept. Pathology
"> || _`\<,_ // \\ \> | "to pay for my hobbies I have to work
` || (_)/ (_) // \\ \_ as an antibody engineer"
