Ex Parte Schneck et al - Page 13

                Appeal 2007-1161                                                                                 
                Application 09/954,166                                                                           
                this argument persuasive because the claims at issue are not limited to how                      
                the claimed complex is utilized.  Harris’s statement, at most, appears to                        
                apply only when antibodies are used in a milieu where certain properties,                        
                such as “complement binding,” would be unwanted (Harris, p. 2, ll. 5-8).                         
                       Appellants also contend that even if there were reason to modify Dal                      
                Porto, “the modification would have been to substitute one of the TCR or                         
                class II MHC extracellular domains for the MHC class I α chain in the                            
                fusion protein, to express the other extracellular domain by itself, and to                      
                permit the two extracellular domains to associate as the prior art taught they                   
                would” (Br. 15).  We do not agree.                                                               
                       In its normal configuration, each of the two TCR extracellular                            
                domains of the T-cell receptor is linked to a unique transmembrane segment                       
                which together form a heterodimer (Specification 4, 8, and Fig. 1A; Findings                     
                of Fact 2).  Chang’s soluble synthetic TCR heterodimer – where the TCR                           
                extracellular domains are appended to peptides which themselves dimerize                         
                together – mimics this normal T-cell receptor configuration.  Thus, the most                     
                logical and normal structure of a soluble synthetic TCR is one in which each                     
                extracellular domain is fused to a separate peptide segment.  The skilled                        
                worker, in adopting Dal Porto’s strategy to enhance the binding affinity of                      
                soluble TCR, would have been motivated to graft one extracellular domain                         
                to the immunoglobulin heavy chain and the other to the light chain in order                      
                to mimic the native TCR configuration.                                                           
                       Moreover, as argued by the Examiner, Chang’s disclosure that                              
                dimerization between soluble TCR subunits can be improved by grafting                            
                each subunit to proteins which themselves associate together would have led                      
                the skilled worker to fuse the second T cell receptor subunit to the                             

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