Appeal No. 94-1483
Application No. 07/695,141
amino acid linker (claim 4). Further, appellants claim
nucleic acids having a sequence coding for a soluble, single
chain polypeptide recited in claim 3 (claim 14).
As explained in the paragraph bridging pages 1 and 2 of
the specification (citations omitted):
The T cell receptor (TCR) is a molecular
complex consisting of multiple subunits that mediate
the recognition of antigen in the context of a
particular major histocompatibility complex (MHC)
product. . . . The antigen/MHC binding moiety,
termed Ti, is a disulfide-linked heterodimer of 90
kD consisting of one " and one $ submit on the
majority of peripheral T lymphocytes. Both subunits
are immunoglobulin-like, being composed of variable
and constant domains, the former encoding the unique
specificity of a given T cell clone. Ti, in turn,
is non-covalently associated with a set of four
invariant monomorphic subunits ((, *, , and .),
collectively termed CD3. All six receptor subunits
are trans-membrane proteins and all but the , and .
subunits possess N-linked glycan moieties. The Ti "
and $ subunits likely form a binding site for
antigen and major histocompatability complex (MHC)
through interaction of their variable domains
whereas the CD3 subunits are thought to subserve
signal transduction functions. In addition, it is
known that a subpopulation of T cells (# 5% of
peripheral T lymphocytes) exist that contain T cell
receptors which contain Ti ( and Ti * subunits that
form heterodimers which form a binding site for
antigen and MHC through interaction of their
variable domains. Furthermore, there is now direct
evidence to show that at least in the case of one
nominal antigen which is a hapten, there is a
subsite on the Ti molecule which directly binds
hapten in the absence of MHC with an affinity
constant of -10- .5
-7-
Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 Next
Last modified: November 3, 2007