Sandbox Reserved 930: Difference between revisions

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==Introduction of the Myosin head S1 ==
==Introduction of the Myosin head S1 ==
<StructureSection load='1B7T' size='450' frame='true' side='right' caption='Myosin subfragment 1' scene='57/579700/Whole_structure/3'>
<StructureSection load='1B7T' size='450' frame='true' side='right' caption='Myosin subfragment 1' scene='57/579700/Whole_structure/3'>
Myosin is a large asymmetric molecule with a MW of about 500,000 kDa. It consist of a long tail and two globular head domains termed myosin subfragment 1 (S1), one neck subfragment 2 (S2) and a light meromyosin tail (LMM) (reference 1). Myosin S1 unit comprises of a motor domain (MD) and a lever arm (Fig.2). By 2000 the structures of three scallop myosin S1 isoforms have been determined (reference 2,3) , which are:  
Myosin is a large asymmetric molecule with a MW of about 500,000 kDa. It consist of two globular head domains termed myosin subfragment 1 (S1), one neck subfragment 2 (S2) and a light meromyosin tail (LMM) <ref>PMID: 8203020</ref>. Myosin S1 unit comprises of a motor domain (MD) and a lever arm (Fig.3). By 2000 the structures of three scallop myosin S1 isoforms have been determined <ref>PMID: 11016966</ref><ref>PMID: 10338210</ref>, which are:  


• S1 nucleotide-free state corresponding to the rigor state of myosin, actin complex (PDB link 1DFK)
• S1 nucleotide-free state corresponding to the rigor state of myosin, actin complex (PDB link 1DFK)
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• S1 Mg-ADP state corresponding to the myosin detached state (1b7t)
• S1 Mg-ADP state corresponding to the myosin detached state (1b7t)


By comparing the available crystal structures of different myosin S1 unit isoforms, it enables us to understand the conformational changes within the motor domain depending on the nucleotide content in the active site.
 
Here mainly the structure and function of MD relevant in the S1 Mg-ADP (pre power stroke) state will be discussed.
By comparing the available crystal structures of different myosin S1 unit isoforms, it enables us to understand the conformational changes within the motor domain depending on the nucleotide content in the active site. Here mainly the structure and function of MD relevant in the S1 Mg-ADP (pre power stroke) state will be discussed.