Award details

Structure and function of a novel functional domain in unconventional myosins

Reference	BB/C004906/1
Principal Investigator / Supervisor	Professor Michelle Peckham
Co-Investigators / Co-Supervisors	Professor Peter Knight
Institution	University of Leeds
Department	Bionanosciences
Funding type	Research
Value (£)	234,182
Status	Completed
Type	Research Grant
Start date	01/06/2005
End date	31/05/2008
Duration	36 months

Abstract

There are over 18 classes of the ubiquitous motor protein called myosin, of which 11 are expressed in humans. Conventional myosin, myosin 2, is a dimmer, and forms filaments via interactions between the extensive coiled-coil domain in its tail. For the other classes of myosins, in the absence of experimental data, a myosin is predicted to form a dimmer if a region of coiled-coil sequence is present, or a monomer if not. There has been much controversy over whether myosins, in particular myosin 6, are in fact monomers or dimmers, as this region of coiled-coil sequence is often very short and highly charged, even in the a and d positions that are classically hydrophobic residues. We have discovered that the first third of the predicted coiled-coil region in myosin 10 does not form a coiled coil, but is in fact a stable single chain a-helix (SAH). This is this first time that this type of structure has been reported for any myosin. It is an unusual structural domain, and has only been reported for two other proteins, caldesmon and the ribosomal protein L9, where it is thought to act as a rigid spacer between neighbouring domains. Sequence homology with other myosins (myosin 6,7a and myoM in Dictyostelium) shows that the SAH domain could also be present in these myosins. Our aim is to investigate the structure of this domain in these other myosins to determine if it is similar to that of myosin 10, to determine if it¿s presence instead of the predicted coiled coil means that the myosin is likely to be monomeric rather than dimeric, and to determine if this structure acts as a rigid spacer and or is able to lengthen the effective lever of myosin.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	Structural Biology
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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