The ATPase activity of Myr3, a rat myosin I, is allosterically inhibited by its own tail domain and by Ca2+ binding to its light chain calmodulin.

Stöffler, H E; Bähler, M

Stöffler, H E; Bähler, M.

Affiliation

Stöffler HE; Adolf-Butenandt-Institut, Zellbiologie, Ludwig-Maximilians-Universität, D-80336 München, Germany.

J Biol Chem ; 273(23): 14605-11, 1998 Jun 05.

Article in En | MEDLINE | ID: mdl-9603977

Subject(s)

Ca(2+) Mg(2+)-ATPase/antagonists & inhibitors; Calcium/pharmacology; Calmodulin/metabolism; Myosin Type I; Myosins/chemistry; Actins/metabolism; Actins/ultrastructure; Allosteric Regulation/physiology; Amino Acid Sequence; Animals; Antibodies/pharmacology; Enzyme Activation/physiology; Immunoglobulin Fab Fragments/pharmacology; Liver/chemistry; Male; Microscopy, Electron; Molecular Sequence Data; Myosin Light Chains/metabolism; Myosins/ultrastructure; Peptide Fragments/chemistry; Rats; Rats, Sprague-Dawley; src Homology Domains/physiology

Search on Google

Add to My VHL

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Calmodulin / Calcium / Myosins / Ca(2/) Mg(2/)-ATPase / Myosin Type I Limits: Animals Language: En Journal: J Biol Chem Year: 1998 Document type: Article Affiliation country: Germany Country of publication: United States

Search on Google

Add to My VHL

XML

PubMed Links