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17919 Ensembl ENSG00000167306 ENSMUSG00000025885 UniProt Q9ULV0 P21271 RefSeq (mRNA) NM_001080467 NM_008661 NM_201600 RefSeq (protein) NP_001073936 n/a Location (UCSC) Chr 18: 49.82 – 50.2 Mb Chr 18: 74.57 – 74.9 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myosin-Vb, a myosin V type protein, is encoded by the MYO5B gene in humans. Recent evidence suggests that Myosin-Vb is ...
Myosin VI is an unconventional myosin motor, which is primarily processive as a dimer, but also acts as a nonprocessive monomer. It walks along actin filaments, travelling towards the pointed end (- end) of the filaments. [44] Myosin VI is thought to transport endocytic vesicles into the cell. [45]
Unconventional myosin-Va is a motor protein in charge of the intracellular transport of vesicles, organelles and protein complexes along the actin filaments. [ 5 ] [ 6 ] [ 7 ] In humans it is coded for by the MYO5A gene .
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 VIIA is an unconventional myosin with the longest tail (1360 aa). The tail is expected to dimerize, resulting in a two-headed molecule. Unconventional myosins have diverse functions in eukaryotic cells and are primarily thought to be involved in the movement or linkage of intra-cellular membranes and organelles to the actin cytoskeleton ...
MYLK’s contain a catalytic core domain with an ATP binding domain. On either sides of the catalytic core sit calcium ion/calmodulin binding sites. Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain is located at the C-Terminus end of the kinase.
The enzyme is composed of three subunits: the catalytic region (protein phosphatase 1, or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function. The catalytic region uses two manganese ions as catalysts to dephosphorylate the light-chains on myosin, which causes a conformational change in the myosin and relaxes ...
Meromyosin is a part of myosin (mero meaning "part of"). With regards to human anatomy myosin and actin constitute the basic functional unit of a muscle fiber, called sarcomere, playing a role in muscle contraction.