Appeal 2007-1161
Application 09/954,166
the immunoglobulin heavy chain in Dal Porto’s molecule is replaced by the
extracellular domain of a first transmembrane protein in the claimed
complex. The first extracellular domain forms a ligand binding site with an
extracellular domain of a second transmembrane protein. The rejection
focuses on the narrower embodiment in which the extracellular domains are
derived from TCR. Secondly, in the claimed molecular complex, the
extracellular domain of the second transmembrane membrane protein is
fused to the immunoglobulin light chain; in Dal Porto’s molecule, the
immunoglobulin light chain is not a fusion protein. (See Br. 13).
The following figure illustrates these differences:
TCR
heterodimer
MHC
Light Light
chain chain
Heavy Heavy
chain chain
Dal Porto Claim 43
The figure depicts the structure of Dal Porto’s molecule contrasted with an
embodiment of claim 43.
Obviousness requires a teaching that all elements of the claimed
invention are found in the prior art and “a reason that would have prompted
a person of ordinary skill in the relevant field to combine the elements in the
way the claimed new invention does.” KSR Int’l Co. v. Teleflex Inc., 127 S.
Ct. 1727, 1741, 82 USPQ2d 1385, 1396 (2007).
Dal Porto teaches that the binding affinity and efficacy of soluble
MHC was improved by grafting the MHC to immunoglobulin heavy chain,
and producing a soluble divalent molecule comprising the chimeric heavy
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