Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function
ISSN: |
0006-291X
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Keywords: |
[abr] COS; cone outer segment ; [abr] PDE; phosphodiesterase ; [abr] PMSF; phenylmethyl-sulfonyl fluoride ; [abr] ROS; rod outer segment ; [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel ; [abr] cGMP; guanosine 3', 5'-cyclic monophosphate
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Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
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Topics: |
Biology
Chemistry and Pharmacology
Physics
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Type of Medium: |
Electronic Resource
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URL: |
_version_ | 1798292258991112192 |
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autor | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
autorsonst | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
book_url | http://dx.doi.org/10.1016/S0006-291X(05)81418-4 |
datenlieferant | nat_lic_papers |
fussnote | Previously, we have domain-mapped the 87 amino acid PDEγ inhibitory subunit of the retinal phosphodiesterase (PDE) αβγ"2complex using synthetic peptides (1). The PDEγ subunit has a binding domain for transducin-α (Tα) and for PDEα/β within residues #24-45. An inhibitory region for PDEα/β is within residues #80-87. In order to establish the role of individual amino acids in the function of the PDEγ inhibitory subunit, mutants were synthesized and utilized in PDE inhibition assays. The following mutants exhibited a decreased ability to inhibit PDEα/β: Tyr"8"4-〉Gly; Arg"2"4-〉Gly; and Arg"3"3-〉Pro. Sequence comparisons with cone PDEγ indicate that there is identity within these functional regions. |
hauptsatz | hsatz_simple |
identnr | NLZ184994578 |
issn | 0006-291X |
journal_name | Biochemical and Biophysical Research Communications |
materialart | 1 |
package_name | Elsevier |
publikationsort | Amsterdam |
publisher | Elsevier |
reference | 181 (1991), S. 306-309 |
schlagwort | [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate |
search_space | articles |
shingle_author_1 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
shingle_author_2 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
shingle_author_3 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
shingle_author_4 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. |
shingle_catch_all_1 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate 0006-291X 0006291X Elsevier |
shingle_catch_all_2 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate 0006-291X 0006291X Elsevier |
shingle_catch_all_3 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate 0006-291X 0006291X Elsevier |
shingle_catch_all_4 | Oppert, B. Gonzalez, K. Hurt, D. Cunnick, J. Takemoto, D. Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate [abr] COS; cone outer segment [abr] PDE; phosphodiesterase [abr] PMSF; phenylmethyl-sulfonyl fluoride [abr] ROS; rod outer segment [abr] SDS-PAGE; sodium dodecyl sulfate polyacrylamide gel [abr] cGMP; guanosine 3', 5'-cyclic monophosphate 0006-291X 0006291X Elsevier |
shingle_title_1 | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function |
shingle_title_2 | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function |
shingle_title_3 | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function |
shingle_title_4 | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function |
sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
timestamp | 2024-05-06T08:45:40.126Z |
titel | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function |
titel_suche | Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function Previously, we have domain-mapped the 87 amino acid PDEγ inhibitory subunit of the retinal phosphodiesterase (PDE) αβγ"2complex using synthetic peptides (1). The PDEγ subunit has a binding domain for transducin-α (Tα) and for PDEα/β within residues #24-45. An inhibitory region for PDEα/β is within residues #80-87. In order to establish the role of individual amino acids in the function of the PDEγ inhibitory subunit, mutants were synthesized and utilized in PDE inhibition assays. The following mutants exhibited a decreased ability to inhibit PDEα/β: Tyr"8"4-〉Gly; Arg"2"4-〉Gly; and Arg"3"3-〉Pro. Sequence comparisons with cone PDEγ indicate that there is identity within these functional regions. |
topic | W V U |
uid | nat_lic_papers_NLZ184994578 |