| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-155 |
Sentence |
denotes |
Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif. |
| T2 |
156-332 |
Sentence |
denotes |
The type II cAMP-dependent protein kinase is localized to specific subcellular environments through the binding of the regulatory subunit (RII) dimer to RII-anchoring proteins. |
| T3 |
333-642 |
Sentence |
denotes |
Computer-aided analysis of secondary structure, performed on four RII-anchoring protein sequences (the microtubule-associated protein 2, P150, and two thyroid proteins Ht 21 and Ht 31), has identified common regions of approximately 14 residues which display high probabilities of forming amphipathic helices. |
| T4 |
643-783 |
Sentence |
denotes |
The potential amphipathic helix region of Ht 31 (Leu-Ile-Glu-Glu-Ala-Ala-Ser-Arg-Ile-Val-Asp-Ala-Val-Ile) lies between residues 494 and 507. |
| T5 |
784-918 |
Sentence |
denotes |
A bacterially expressed 318-amino acid fragment, Ht 31 (418-736), containing the amphipathic helix region, was able to bind RII alpha. |
| T6 |
919-1048 |
Sentence |
denotes |
Site-directed mutagenesis designed to disrupt the secondary structure in the putative binding helix reduced binding dramatically. |
| T7 |
1049-1208 |
Sentence |
denotes |
Specifically, substitution of proline for Ala-498 significantly diminished RII alpha binding, and similar mutation of Ile-502 or Ile-507 abolished interaction. |
| T8 |
1209-1341 |
Sentence |
denotes |
Mutation of Ala-522 to proline, which is located outside the predicted amphipathic helix region, had no effect on RII alpha binding. |
| T9 |
1342-1448 |
Sentence |
denotes |
These data suggest that anchoring proteins interact with RII alpha via an amphipathic helix binding motif. |
| T1 |
0-155 |
Sentence |
denotes |
Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif. |
| T2 |
156-332 |
Sentence |
denotes |
The type II cAMP-dependent protein kinase is localized to specific subcellular environments through the binding of the regulatory subunit (RII) dimer to RII-anchoring proteins. |
| T3 |
333-642 |
Sentence |
denotes |
Computer-aided analysis of secondary structure, performed on four RII-anchoring protein sequences (the microtubule-associated protein 2, P150, and two thyroid proteins Ht 21 and Ht 31), has identified common regions of approximately 14 residues which display high probabilities of forming amphipathic helices. |
| T4 |
643-783 |
Sentence |
denotes |
The potential amphipathic helix region of Ht 31 (Leu-Ile-Glu-Glu-Ala-Ala-Ser-Arg-Ile-Val-Asp-Ala-Val-Ile) lies between residues 494 and 507. |
| T5 |
784-918 |
Sentence |
denotes |
A bacterially expressed 318-amino acid fragment, Ht 31 (418-736), containing the amphipathic helix region, was able to bind RII alpha. |
| T6 |
919-1048 |
Sentence |
denotes |
Site-directed mutagenesis designed to disrupt the secondary structure in the putative binding helix reduced binding dramatically. |
| T7 |
1049-1208 |
Sentence |
denotes |
Specifically, substitution of proline for Ala-498 significantly diminished RII alpha binding, and similar mutation of Ile-502 or Ile-507 abolished interaction. |
| T8 |
1209-1341 |
Sentence |
denotes |
Mutation of Ala-522 to proline, which is located outside the predicted amphipathic helix region, had no effect on RII alpha binding. |
| T9 |
1342-1448 |
Sentence |
denotes |
These data suggest that anchoring proteins interact with RII alpha via an amphipathic helix binding motif. |