Myosin head, motor domain-like
IPR001609
Definition
Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains PMID:1939027, 2 alkali light chains, and 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail, 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 PMID:2806546. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy PMID:3540939. The 3-D structure of the head portion of myosin has been determined PMID:8316857 and a model for actin-myosin complex has been constructed PMID:8316858. The globular head is well conserved, some highly-conserved regions possibly relating to functional and structural domains PMID:6576334. The rod-like tail starts with an invariant proline residue, and contains many repeats of a 28 residue region, interrupted at 4 regularly-spaced points known as skip residues. Although the sequence of the tail is not well conserved, the chemical character is, hydrophobic, charged and skip residues occuring in a highly ordered and repeated fashion PMID:6576334. This domain is also found in chitinases present in filamentous fungi, enzymes that play a critical role in promoting the synthesis of chitin at the hyphal tip, thus influencing fungal growth and the architecture of fungal infection structures [[cite:PMID:31681248], [cite:PMID:22964252]].
39 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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