Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Glycoprotein – e.g. – mucins – proteoglycans – etc.
Reexamination Certificate
2005-10-04
2005-10-04
Chan, Christina (Department: 1644)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Glycoprotein, e.g., mucins, proteoglycans, etc.
C530S402000
Reexamination Certificate
active
06951927
ABSTRACT:
The invention relates to novel proteins with novel integrin and I domain activity and nucleic acids encoding these proteins. The invention further relates to the use of the novel proteins in the treatment of integrin related disorders.TABLE 1Computationally designed mutantsaWTido1qido1rido2rjlm2rBackboneEnergyb1ido−1037 −1145−1138−1116 −6781jlm−1059+82758 −840−1000−1086PositionResidues139I——V—153M——A—156FLW——157V——I—160VI———199VIII—215ILL—V219V———I223F———L238VFFII239VLLL—240ILL——259ALL——269IL———271VF———287IVVV—299VAII—308IV———aMutants are named according to the structure that was stabilized (ido or jlm), the solvation potential used (1 or 2) and the definition of core residues (q or r).bThe lowest energy rotamer configuration was calculated for each sequence in the lido structure, and cross-calculated in the ljlm structure, using both solvent potentials; all 50 core residues were used in order to make the q and r energies comparable. Results are shown for solvent potential 1 and were similar for potential 2.# A severe clash of the side-chain of F271 with the backbone caused the high energy of the 1q sequence in the 1jlm structure; no movement of the backbone is allowed by the design method.
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Mayo Stephen
Shifman Julia
Shimaoka Motomu
Springer Timothy
California Institute of Technology
Chan Christina
Dorsey & Whitney LLP.
Haddad Maher
Kosslak, Esq. Renee M.
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