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

Crystal structure of calmodulin.

R H Kretsinger, S E Rudnick, L J Weissman

    Journal of Inorganic Biochemistry
    |October 1, 1986
    PubMed
    Summary
    This summary is machine-generated.

    The crystal structure of calmodulin reveals a dumbbell shape with two pairs of domains connected by a flexible handle. Hydrophobic patches on the surface suggest binding sites for target proteins.

    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

    BIFURCATING DISTRIBUTIVE SYSTEM USING MONTE CARLO METHOD.

    Mathematical and computer modelling·2012
    Same author

    Structural analysis of leucine-rich-repeat variants in proteins associated with human diseases.

    Cellular and molecular life sciences : CMLS·2005
    Same author

    3-Deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia coli. Model of binding of phosphoenolpyruvate and D-arabinose-5-phosphate.

    Journal of molecular biology·2000
    Same author

    Structure of 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis.

    Journal of molecular biology·2000
    Same author

    Membrane-bound 3D structures reveal the intrinsic flexibility of annexin VI.

    Journal of structural biology·2000
    Same author

    Super-motifs and evolution of tandem leucine-rich repeats within the small proteoglycans--biglycan, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin.

    Proteins·2000

    Area of Science:

    • Structural Biology
    • Biochemistry

    Background:

    • Calmodulin is a crucial calcium-binding protein involved in numerous cellular processes.
    • Understanding calmodulin's structure is key to elucidating its function and interactions.

    Purpose of the Study:

    • To determine the high-resolution crystal structure of calmodulin.
    • To identify structural features related to calmodulin's function and protein binding.

    Main Methods:

    • X-ray diffraction crystallography to determine the 3D structure.
    • Analysis of polypeptide chain tracing and side chain identification.
    • Comparison with related proteins like troponin C.

    Main Results:

    • The calmodulin structure reveals a dumbbell-shaped molecule approximately 65 A long and 30 A in diameter.

    Related Experiment Videos

  • Two homologous domain pairs (1-2 and 3-4) are connected by a flexible alpha-helical handle (residues 67-93).
  • Distinct hydrophobic patches, bordered by anionic residues, are present on the surface of both domain pairs, indicating potential protein interaction sites.

    • Conclusions:

    • The determined crystal structure provides detailed insights into calmodulin's architecture.
    • The identified hydrophobic surfaces are proposed as key interaction sites for calmodulin target proteins.
    • Structural similarities and differences with troponin C highlight conserved and unique features in calcium-binding proteins.