Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Conservation within the myosin motor domain: implications for structure and function

M J Cope1, J Whisstock, I Rayment

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, England.

Structure (London, England : 1993)
|August 15, 1996
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Understanding CD30 biology and therapeutic targeting: a historical perspective providing insight into future directions.

Blood cancer journal·2017
Same author

Overexpression of myosin VI in prostate cancer cells enhances PSA and VEGF secretion, but has no effect on endocytosis.

Oncogene·2009
Same author

Structure of southern bean mosaic virus at 2.8 A resolution.

Nature·2009
Same author

The phospholipase A(2) inhibitor methyl indoxam suppresses diet-induced obesity and glucose intolerance in mice.

British journal of pharmacology·2009
Same author

Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli.

Plasmid·2008
Same author

Actin-targeting natural products: structures, properties and mechanisms of action.

Cellular and molecular life sciences : CMLS·2006
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

This study details conserved residues in myosin motor domains, revealing at least thirteen classes. It maps these residues to structures, aiding understanding of actin binding and ATP hydrolysis mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Myosins are ATP-dependent molecular motors that interact with actin filaments.
  • The precise actin-binding site and mechanisms of force generation remain incompletely understood.
  • Previous studies identified approximately twelve myosin classes based on motor domain phylogeny.

Purpose of the Study:

  • To analyze conserved residues within the myosin motor domain in detail.
  • To relate conserved residues to known myosin structures.
  • To elucidate the functional significance of conserved residues in myosin-actin interactions and ATP hydrolysis.

Main Methods:

  • Phylogenetic analysis of myosin motor domains.
  • Mapping conserved residues onto available crystal structures of myosins.

Related Experiment Videos

  • Comparative analysis of residue conservation across different myosin classes.

    • Main Results:

    • Identification of at least thirteen distinct myosin classes.
    • Localization of conserved residues within the 3D structural framework of the myosin motor domain.
    • Observation of poor conservation at the putative actin-binding site, with identification of several highly conserved, potentially functionally critical residues.

    Conclusions:

    • Sequence analysis provides a valuable framework for interpreting X-ray structures of complex proteins.
    • The functional significance of conserved and mutated residues can be assessed by mapping them onto structural models.
    • This approach aids in understanding the molecular mechanisms of motor proteins like myosins.