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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Morales, Manuel F. Onishi, Hirofumi Mikhailenko, Sergey V. |
| Description | Author Affiliation: Onishi H ( ERATO Actin Filament Dynamics Project, Japan Science and Technology Agency, c/o RIKEN SPring-8 Center, Kouto, Sayo, Hyogo 679-5148, Japan.); |
| Abstract | To understand the complicated interplay when a traveling myosin head reaches interaction distance with two actins in a filament we looked to three myosin loops that early on exert their influences from the 'outside' of the myosin. On these we conduct, functionally test, and interpret strategically chosen mutations at sites thought from crystallography to be a patch for binding the 'first' of the two actins. One loop bears a hydrophobic triplet of residues, one is the so-called 'loop 2,' and the third is the 'cardiomyopathy' loop. So far as we know, the myosin sites that first respond are the two lysine-rich loops that produce an ionic strength-dependent weak-binding complex with actin. Subsequently, the three loops of interest bind the first actin simultaneously, and all three assist in closing the cleft in the 50-kDa domain of the myosin, a closure that results in transition from weak to strong binding and precedes rapid Pi release and motility. Mutational analysis shows that each such loop contact is distinctive in the route by which it communicates with its specific target elsewhere in myosin. The strongest contact with actin, for example, is that of the triplet-bearing loop. On the other hand, that of loop 2 (dependent on drawing close two myosin lysines and two actin aspartates) is probably responsible for opening switch I and uncovering the gamma-phosphate moiety of bound ATP. Taking into account these findings, we begin to arrange in order many molecular events in muscle function. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 16 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Chemistry Myosins Amino Acid Substitution Animals Cardiomyopathies Enzymology DNA Mutational Analysis Enzyme Activation Hydrophobic And Hydrophilic Interactions Mutation Genetics Protein Conformation Pyrenes Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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