Kinase anchor protein muteins, peptides thereof and related documents
First Claim
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1. A polypeptide that is a mutein of SEQ ID NO:
- 2, wherein the mutein exhibits modified binding to a regulatory subunit of PKA compared to SEQ ID NO;
2 and wherein said mutein;
is a peptide selected from the group consisting of a) a peptide having the sequence SEQ ID NO;
2, b) a peptide having the sequence SEQ ID NO;
2 further comprising a C-terminal cysteine, c) a peptide having the sequence SEQ ID NO;
2 wherein residues 1-8 are deleted, and d) a peptide having the sequence SEQ ID NO;
2 wherein residues 1-8 are deleted further comprising a C-terminal cysteine;
except that said peptide has an amino acid residue substitution at the residue equivalent to residue 21 of SEQ ID NO;
2 of Trp and/or Ile for Val, or an amino acid residue substitution at the residue equivalent to residue 12 of SEQ ID NO;
2 of Phe for Leu; and
zero, one, or two amino acid residue substitutions selected from the group consisting of Phe, Ile, Leu, Val, His, Met, Arg, Thr, Trp, or Tyr at the residue equivalent to residue 9 of SEQ ID NO;
2 for Gln; and
Phe, Ile, Leu, Thr, Val, Trp, or Tyr at the residue equivalent to residue 25 of SEQ ID NO;
2 for Met.
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Abstract
A-kinase anchor protein (AKAPs) muteins, peptides thereof, and nucleic acids encoding the peptides are provided herein. Also provided are transgenic animals, cells comprising transgenes and various methods employing such peptides.
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Citations
17 Claims
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1. A polypeptide that is a mutein of SEQ ID NO:
- 2, wherein the mutein exhibits modified binding to a regulatory subunit of PKA compared to SEQ ID NO;
2 and wherein said mutein;is a peptide selected from the group consisting of a) a peptide having the sequence SEQ ID NO;
2, b) a peptide having the sequence SEQ ID NO;
2 further comprising a C-terminal cysteine, c) a peptide having the sequence SEQ ID NO;
2 wherein residues 1-8 are deleted, and d) a peptide having the sequence SEQ ID NO;
2 wherein residues 1-8 are deleted further comprising a C-terminal cysteine;except that said peptide has an amino acid residue substitution at the residue equivalent to residue 21 of SEQ ID NO;
2 of Trp and/or Ile for Val, or an amino acid residue substitution at the residue equivalent to residue 12 of SEQ ID NO;
2 of Phe for Leu; andzero, one, or two amino acid residue substitutions selected from the group consisting of Phe, Ile, Leu, Val, His, Met, Arg, Thr, Trp, or Tyr at the residue equivalent to residue 9 of SEQ ID NO;
2 for Gln; and
Phe, Ile, Leu, Thr, Val, Trp, or Tyr at the residue equivalent to residue 25 of SEQ ID NO;
2 for Met. - View Dependent Claims (2, 3, 4, 5, 6, 7, 9, 10, 11, 12, 13, 14, 17)
- 2, wherein the mutein exhibits modified binding to a regulatory subunit of PKA compared to SEQ ID NO;
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8. A peptide that has enhanced ability to bind to PKA-RIα
- subunit, and a reduced ability to bind to PKA-RIIα
subunit, compared to the peptide of SEQ ID NOs;
1 or 2, wherein the peptide is selected from the group consisting of;
- subunit, and a reduced ability to bind to PKA-RIIα
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15. A peptide that has an enhanced ability to bind to PKA-RIα
- subunit, and a reduced ability to bind to PKA-RIIα
subunit, compared to the peptide of SEQ ID NOs;
1 or 2, wherein the peptide is selected from the group consisting of;
- subunit, and a reduced ability to bind to PKA-RIIα
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16. A peptide that binds to the PKA-RIα
- subunit but has substantially no ability to bind to the PKA-RIIα
subunit, compared to the peptide of SEQ ID NOs;
1 or 2, wherein the peptide is
- subunit but has substantially no ability to bind to the PKA-RIIα
Specification