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PROSITE documentation PDOC51844 [for PROSITE entry PS51844]

Myosin N-terminal SH3-like domain profile





Description

Members of the myosin superfamily of actin-based motors act in a variety of cellular functions such as muscle contraction, cell and organelle movement, membrane trafficking, and signal transduction. Although myosin motor domains (see <PDOC51456>) show a high degree of sequence conservation, the individual myosin classes are clearly defined by differences in the head structure. The N-terminal region of myosins from different classes varies greatly in length and amino acid composition among the individual members. Many myosins have an SH3-like domain at the N-terminus of the motor domain. This includes myosins in classes II, V, VI, XI, XXII and XXIV. The myosin N-terminal SH3-like domain may mediate some aspect of the conformational communication that occurs within the myosin head during actin and nucleotide binding. Part of this effect may be mediated through interactions with the neck-associated essential light chains that are in close proximity to this portion of the head domain and also transiently interact with actin [1,2,3,4].

The myosin N-terminal SH3-like domain comprises ~50 amino acids and forms a protruding, six-stranded, antiparallel, β-barrel domain (see <PDB:1OE9>) with similarities to the SH3 domain (see <PDOC50002>) [1,5].

The profile we developed covers the entire myosin N-terminal SH3-like domain.

Last update:

October 2017 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

SH3_LIKE, PS51844; Myosin N-terminal SH3-like domain profile  (MATRIX)


References

1AuthorsFujita-Becker S. Tsiavaliaris G. Ohkura R. Shimada T. Manstein D.J. Sutoh K.
TitleFunctional characterization of the N-terminal region of myosin-2.
SourceJ. Biol. Chem. 281:36102-36109(2006).
PubMed ID16982629
DOI10.1074/jbc.M605171200

2AuthorsLowey S. Saraswat L.D. Liu H. Volkmann N. Hanein D.
TitleEvidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins.
SourceJ. Mol. Biol. 371:902-913(2007).
PubMed ID17597155
DOI10.1016/j.jmb.2007.05.080

3AuthorsMooseker M.S. Foth B.J.
TitleThe structural and functional diversity of the myosin family of actin-based molecular motors.
Source(In) Myosins, Proteins and Cell Regulation, Vol 7, pp1-34, Springer, Dordrecht (2008).

4AuthorsHeintzelman M.B. Enriquez M.E.
TitleMyosin diversity in the diatom Phaeodactylum tricornutum.
SourceCytoskeleton 67:142-151(2010).
PubMed ID20217677
DOI10.1002/cm.20431

5AuthorsMenetrey J. Bahloul A. Wells A.L. Yengo C.M. Morris C.A. Sweeney H.L. Houdusse A.
TitleThe structure of the myosin VI motor reveals the mechanism of directionality reversal.
SourceNature 435:779-785(2005).
PubMed ID15944696
DOI10.1038/nature03592



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