Retinal cyclic-GMP phosphodiesterase γ-subunit: Use of mutant synthetic peptides to define function

ISSN:
0006-291X
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
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798292258991112192
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
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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
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uid nat_lic_papers_NLZ184994578