Publication Date:
1988-09-23
Description:
Complementary DNAs were isolated and used to deduce the primary structures of the alpha 1 and alpha 2 subunits of the dihydropyridine-sensitive, voltage-dependent calcium channel from rabbit skeletal muscle. The alpha 1 subunit, which contains putative binding sites for calcium antagonists, is a hydrophobic protein with a sequence that is consistent with multiple transmembrane domains and shows structural and sequence homology with other voltage-dependent ion channels. In contrast, the alpha 2 subunit is a hydrophilic protein without homology to other known protein sequences. Nucleic acid hybridization studies suggest that the alpha 1 and alpha 2 subunit mRNAs are expressed differentially in a tissue-specific manner and that there is a family of genes encoding additional calcium channel subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellis, S B -- Williams, M E -- Ways, N R -- Brenner, R -- Sharp, A H -- Leung, A T -- Campbell, K P -- McKenna, E -- Koch, W J -- Hui, A -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458626" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Base Sequence
;
Calcium/*metabolism
;
Calcium Channel Blockers/pharmacology
;
Cloning, Molecular
;
*Dna
;
DNA Restriction Enzymes
;
Dihydropyridines/pharmacology
;
*Ion Channels/drug effects
;
Molecular Sequence Data
;
Organ Specificity
;
*Peptide Mapping
;
RNA, Messenger/biosynthesis
;
Rabbits
;
Sequence Homology, Nucleic Acid
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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