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

Ras-binding domains: predicting function versus folding

G Kalhammer1, M Bähler, F Schmitz

  • 1Adolf-Butenandt-Institut/Zellbiologie, Ludwig-Maximilians-Universität München, Germany.

FEBS Letters
|October 10, 1997
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

Pathological complete response with neoadjuvant pembrolizumab and chemotherapy in non-metastatic triple-negative inflammatory breast cancer.

ESMO open·2026
Same author

[Intravesical oxybutynin treatment for neurogenic detrusor overactivity : Efficacy and safety data from clinical practice with the first intravesical oxybutynin treatment authorized in Germany].

Urologie (Heidelberg, Germany)·2024
Same author

[Endocarditis and ischemic stroke of rare cause].

Innere Medizin (Heidelberg, Germany)·2024
Same author

Maternal environmental enrichment protects neonatal brains from hypoxic-ischemic challenge by mitigating brain energetic dysfunction and modulating glial cell responses.

Experimental neurology·2024
Same author

[Flexible assertive community treatment (FACT) as part of a community (health) network].

Tijdschrift voor psychiatrie·2020
Same author

[Reaction on 'Faster recovery of work participation through collaboration between specialist mental health care and Employee Insurance Agency (UWV): a pilot study'].

Tijdschrift voor psychiatrie·2019
Same journal

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same journal

The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

FEBS letters·2026
Same journal

Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

FEBS letters·2026
Same journal

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026
Same journal

α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.

FEBS letters·2026
Same journal

Modelling stem cell differentiation related processes-A practical overview for biologists.

FEBS letters·2026
See all related articles

A newly identified Ras-binding motif in myr 5 protein does not bind Ras. Structural analysis reveals key charge differences, highlighting that similar protein structures do not guarantee similar functions.

Area of Science:

  • Molecular biology
  • Protein interactions
  • Structural biology

Background:

  • Ras proteins are key signaling molecules that interact with various effector proteins.
  • A novel family of Ras-binding domains was recently identified using sequence and motif searches.
  • The myr 5 protein, an unconventional myosin, was predicted to contain a Ras-binding domain.

Purpose of the Study:

  • To investigate the direct binding interaction between the predicted Ras-binding domain of myr 5 and Ras.
  • To understand the structural basis for potential Ras-binding in myr 5.
  • To evaluate the reliability of the identified Ras-binding motif in predicting functional Ras-binding domains.

Main Methods:

  • Direct binding experiments were performed between the proposed Ras-binding domain of myr 5 and Ras.

Related Experiment Videos

  • Molecular modeling was utilized to analyze the structural conformation of the myr 5 domain.
  • Surface charge distribution of the myr 5 domain was compared to known Ras-binding domains.
  • Main Results:

    • Direct binding experiments showed no interaction between the myr 5 domain and Ras.
    • Molecular modeling indicated that the myr 5 domain shares a similar fold with the Ras-binding domain of Raf kinase.
    • The myr 5 domain lacks the crucial positive surface charges present in the Raf kinase Ras-binding domain, which are necessary for interacting with the negatively charged Ras.

    Conclusions:

    • The identified Ras-binding motif in myr 5 does not confer Ras-binding capability.
    • Structural similarity alone is insufficient to predict functional protein-protein interactions.
    • This study demonstrates the functional diversity of proteins with similar structural domains and cautions against over-reliance on motif-based prediction of binding partners.