Myosin head (original) (raw)
The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin. Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament. Myosin exists as a hexamer of two heavy chains, two alkali light chains, and two regulatory light chains. The heavy chain can be subdivided into the globular head at the N-terminal and the coiled-coil rod-like tail at the C-terminal, although some forms have a globular region in their C-terminal.
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|---|---|
| dbo:abstract | The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin. Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament. Myosin exists as a hexamer of two heavy chains, two alkali light chains, and two regulatory light chains. The heavy chain can be subdivided into the globular head at the N-terminal and the coiled-coil rod-like tail at the C-terminal, although some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy. The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed. The globular head is well conserved, and is key to contraction. Muscle contraction results from an attachment–detachment cycle between the myosin heads extending from myosin filaments and the sites on actin filaments. The myosin head first attaches to actin together with the products of ATP hydrolysis, performs a power stroke associated with release of hydrolysis products, and detaches from actin upon binding with new ATP. The detached myosin head then hydrolyses ATP, and performs a recovery stroke to restore its initial position. The strokes have been suggested to result from rotation of the lever arm domain around the converter domain, while the catalytic domain remains rigid. (en) |
| dbo:symbol | Myosin_head |
| dbo:thumbnail | wiki-commons:Special:FilePath/PDB_1kk7_EBI.jpg?width=300 |
| dbo:wikiPageID | 32116201 (xsd:integer) |
| dbo:wikiPageLength | 5824 (xsd:nonNegativeInteger) |
| dbo:wikiPageRevisionID | 1043611292 (xsd:integer) |
| dbo:wikiPageWikiLink | dbr:Protein-protein_interaction dbr:Genetic_code dbr:Energy dbr:Gene_regulation dbr:Myosin dbr:Actin dbr:Muscle_contraction dbr:Protein_complex dbr:Myofilament dbr:Protein_filament dbc:Protein_domains dbr:ATP_hydrolysis dbr:Coiled_coil dbr:Tertiary_structure dbr:Polymer dbr:Isoforms |
| dbp:caption | Scallop myosin in the near-rigor conformation (en) |
| dbp:cdd | cd00124 (en) |
| dbp:interpro | IPR001609 (en) |
| dbp:name | Myosin_head (en) |
| dbp:pfam | PF00063 (en) |
| dbp:pfamClan | CL0023 (en) |
| dbp:prosite | PDOC00017 (en) |
| dbp:scop | 1 (xsd:integer) |
| dbp:symbol | Myosin_head (en) |
| dbp:wikiPageUsesTemplate | dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist |
| dcterms:subject | dbc:Protein_domains |
| rdf:type | owl:Thing dbo:Biomolecule wikidata:Q206229 wikidata:Q8054 yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity dbo:Protein yago:SocialGroup107950920 yago:Unit108189659 |
| rdfs:comment | The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin. Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament. Myosin exists as a hexamer of two heavy chains, two alkali light chains, and two regulatory light chains. The heavy chain can be subdivided into the globular head at the N-terminal and the coiled-coil rod-like tail at the C-terminal, although some forms have a globular region in their C-terminal. (en) |
| rdfs:label | Myosin head (en) |
| owl:sameAs | freebase:Myosin head wikidata:Myosin head https://global.dbpedia.org/id/2L5Mh |
| prov:wasDerivedFrom | wikipedia-en:Myosin_head?oldid=1043611292&ns=0 |
| foaf:depiction | wiki-commons:Special:FilePath/PDB_1kk7_EBI.jpg |
| foaf:isPrimaryTopicOf | wikipedia-en:Myosin_head |
| is dbo:wikiPageWikiLink of | dbr:Meromyosin dbr:Systole dbr:Myosin dbr:Muscular_system dbr:Myofilament dbr:Smooth_muscle dbr:Sarcomere dbr:Myofibril dbr:Skeletal_muscle dbr:Unconventional_myosin-VI |
| is foaf:primaryTopic of | wikipedia-en:Myosin_head |
